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Polymers

Polymers

Polymer is a generic term used to describe a very long molecule consisting of structural units and repeating units connected by covalent chemical bonds. The key feature that distinguishes polymers from other molecules is the repetition of many identical, similar, or complementary molecular subunits in these chains. These subunits, the monomers, are small molecules of low to moderate molecular weight, and are linked to each other during a chemical reaction called polymerization. Instead of being identical, similar monomers can have varying chemical substituents. The differences between monomers can affect properties such as solubility, flexibility, and strength. In proteins, these differences give the polymer the ability to adopt a biologically-active conformation in preference to others. (See self-assembly.) Identical monomers with nonreactive side groups result in a polymer chain that will tend to adopt a random coil conformation, as described by an ideal chain mathematical model. Although most polymers are organic, with carbon-based monomers, there are also inorganic polymers; for example, the silicones, with a backbone of alternating silicon and oxygen atoms. Polymers are typically classified according to three main groups:
- thermoplastics (linear or branched chains)
- thermosets (crosslinked chains)
- elastomers The term polymer covers a large, diverse group of molecules, including substances from proteins to stiff, high-strength Kevlar fibres. For example, the formation of polyethene (also called polyethylene) involves thousands of ethene molecules bonded together to form a straight (or branched) chain of repeating -CH₂-CH₂- units (with a -CH₃ at each terminal): image:example_polymerization.png Polymers are often named in terms of the monomer from which they are made. Because it is synthesized from ethene in a process during which all the double bonds in the vinyl monomers are lost, polyethene has the unsaturated structure: image:polyethene_monomer.png If it were named according to its final structure, it would have the alkane designation "polyethane". Because synthetic polymer formation is governed by random assembly from the constituent monomers, polymer chains within a solution or substance are generally not of equal length. This is unlike basic, smaller molecules in which every atom is stoichiometrically accounted for, and each molecule has a set molecular mass. An ensemble of differing chain lengths, often obeying a normal (Gaussian) distribution, occurs because polymer chains terminate during polymerization after random amounts of chain lengthening (propagation). Proteins are polymers of amino acids. Typically, hundreds of the (nominally) twenty different amino acid monomers make up a protein chain, and the sequence of monomers determines its shape and biological function. (There are also shorter oligopeptides which function as hormones.) But there are active regions, surrounded by, as is believed now (Aug 2003), structural regions, whose sole role is to expose the active regions. (There may be more than one on a given protein.) So the exact sequence of amino acids in certain parts of the chains can vary from species to species, and even given mutations within a species, so long as the active sites are properly accessible. Also, whereas the formation of polyethylene occurs spontaneously under the right conditions, the synthesis of biopolymers such as proteins and nucleic acids requires the help of enzyme catalysts, substances that facilitate and accelerate reactions. Unlike synthetic polymers, these biopolymers have exact sequences and lengths. (This does not include the carbohydrates.) Since the 1950s, catalysts have also revolutionised the development of synthetic polymers. By allowing more careful control over polymerization reactions, polymers with new properties, such as the ability to emit coloured light, have been manufactured. The characterization of a polymer requires several parameters which need to be specified. This is because a polymer actually consists of a statistical distribution of chains of varying lengths, and each chain consists of monomer residues which affect its properties. Some of these parameters are described below.

Physical properties of polymers

Physical properties of polymers include the degree of polymerization, molar mass distribution, crystallinity, as well as the thermal phase transitions:
- T_g, glass transition temperature
- T_m, melting point (for thermoplastics).

Branching

During the propagation of polymer chains, branching can occur. In free-radical polymerization, this occurs when a chain curls back and bonds to an earlier part of the chain. When this curl breaks, it leaves small chains sprouting from the main carbon backbone. Branched carbon chains cannot line up as close to each other as unbranched chains can. This causes less contact between atoms of different chains, and fewer opportunities for induced or permanent dipoles to occur. A low density results from the chains being further apart. Lower melting points and tensile strengths are evident, because the intermolecular bonds are weaker and require less energy to break. Besides branching, polymers can have other topologies: linear, network (cross-linked 3D structure), IPN (integrated polymer network), comb, or star as well as dendrimer and hyperbranched structures.

Stereoregularity

Stereoregularity or tacticity describes the isomeric arrangement of functional groups on the backbone of carbon chains. Isotactic chains are defined as having substituent groups aligned in one direction. This enables them to line up close to each other, creating crystalline areas and resulting in highly rigid polymers. In contrast, atactic chains have randomly aligned substituent groups. The chains do not fit together well and the intermolecular forces are low. This leads to a low density and tensile strength, but a high degree of flexibility. Syndiotactic substituent groups alternate regularly in opposite directions. Because of this regularity, syndiotactic chains can position themselves close to each other, though not as close as isotactic polymers. Syndiotactic polymers have better impact strength than isotactic polymers because of the higher flexibility resulting from their weaker intermolecular forces.

Constitution of polymers

Copolymers

Copolymerization with two or more different monomers results in chains with varied properties. There are twenty amino acid monomers whose sequence results in different shapes and functions of protein chains. Copolymerising ethene with small amounts of 1-hexene (or 4-methyl-1-pentene) is one way to form linear low-density polyethene (LLDPE). (See polyethylene.) The C₄ branches resulting from the hexene lower the density and prevent large crystalline regions from forming within the polymer, as they do in HDPE. This means that LLDPE can withstand strong tearing forces whilst remaining flexible. A block copolymer is formed when the reaction is carried out in a stepwise manner, leading to a structure with long sequences or blocks of one monomer alternating with long sequences of the other. There are also graft copolymers, in which entire chains of one kind (e.g., polystyrene) are made to grow out of the sides of chains of another kind (e.g., polybutadiene), resulting in a product that is less brittle and more impact-resistant. Thus, block and graft copolymers can combine the useful properties of both constituents and often behave as quasi-two-phase systems. The following is an example of step-growth polymerization, or condensation polymerization, in which a molecule of water is given off and nylon is formed. The properties of the nylon are determined by the R and R' groups in the monomers used. nylon The first commercially successful, completely synthetic polymer was nylon 6,6, with alkane chains R = 4C (adipic acid) and R' = 6C (hexamethylene diamine). Including the two carboxyl carbons, each monomer donates 6 carbons; hence the name. In naming nylons, the number of carbons from the diamine is given first and the number from the diacid second. Kevlar is an aromatic nylon in which both R and R' are benzene rings. Copolymers illustrate the point that the repeating unit in a polymer, such as a nylon, polyester or polyurethane, is often made up of two (or more) monomers.

Chemical properties of polymers

Intermolecular forces

The attractive forces between polymer chains play a large part in determining a polymer's properties. Because polymer chains are so long, these interchain forces are amplified far beyond the attractions between conventional molecules. Also, longer chains are more amorphous (randomly oriented). Polymers can be visualised as tangled spaghetti chains - pulling any one spaghetti strand out is a lot harder the more tangled the chains are. These stronger forces typically result in high tensile strength and melting points. The intermolecular forces in polymers are determined by dipoles in the monomer units. Polymers containing amide groups can form hydrogen bonds between adjacent chains; the positive hydrogen atoms in N-H groups of one chain are strongly attracted to the oxygen atoms in C=O groups on another. These strong hydrogen bonds result in, for example, the high tensile strength and melting point of kevlar. Polyesters have dipole-dipole bonding between the oxygen atoms in C=O groups and the hydrogen atoms in H-C groups. Dipole bonding is not as strong as hydrogen bonding, so ethene's melting point and strength are lower than kevlar's, but polyesters have greater flexibility. Ethene, however, has no permanent dipole. The attractive forces between polyethene chains arise from weak van der Waals forces. Molecules can be thought of as being surrounded by a cloud of negative electrons. As two polymer chains approach, their electron clouds repel one another. This has the effect of lowering the electron density on one side of a polymer chain, creating a slight positive dipole on this side. This charge is enough to actually attract the second polymer chain. Van der Waals forces are quite weak, however, so polyethene melts at low temperatures.

Polymer characterization

A variety of lab techniques are used to determine the properties of polymers. Techniques such as wide angle X-ray scattering, small angle X-ray scattering, and small angle neutron scattering are used to determine the crystalline structure of polymers. Gel permeation chromatography is used to determine the number average molecular weight, weight average molecular weight, and polydispersity. FTIR is used to determine composition. Thermal properties such as the glass transition temperature and melting point can be determined by differential scanning calorimetry and dynamic mechanical analysis. Pyrolysis followed by analysis of the fragments is one more technique for determining the possible structure of the polymer. Polymer known as polymer substrate is used for everyday banknotes in Australia and New Zealand, and is also used in commemorative notes in other countries. See also: Polymerization -- Biopolymer -- Condensation polymer -- Addition polymer -- Synthetic polymer -- Glass transition temperature -- Polymer physics -- Important publications in polymer chemistry

External links

- [http://www.borealisgroup.com/public/dictionary/Dictionary.jsp Polymer dictionary]
- [http://www.vivamer.com/ Responsive Biopolymers for Drug Delivery and Imaging]
- [http://web.umr.edu/~wlf/ Polymer Chemistry Hypertext, Educational resource]
- [http://www.polychemistry.com/ Polymer Chemistry Innovations]
- [http://www.odcad.com/html/organicdevice_appearance1.HTM Materials for Organic devices]
- [http://www.pslc.ws/macrog/index.htm The Macrogalleria - a cyberwonderland of polymer fun!] Category:Polymers Category:Polymer chemistry ko:중합체 ms:Polimer ja:重合体 th:โพลีเมอร์

Molecule

A molecule is the smallest particle of a pure chemical substance that still retains its chemical composition and properties. The science of molecules is called molecular chemistry or molecular physics, depending on the focus. Molecular chemistry deals with the laws governing the interaction between molecules that results in the formation and breakage of chemical bonds, while molecular physics deals with the laws governing their structure and properties. In practice, however, this distinction is vague. According to the strict definition, molecules can consist of one atom (as in noble gases) or more atoms bonded together. The concept of monatomic (single-atom) molecule is used almost exclusively in the kinetic theory of gases. In molecular sciences, a molecule consists of a stable system (bound state) comprising two or more atoms. The term unstable molecule is used for very reactive species, i.e., short-lived assemblies (resonances) of electrons and nuclei, such as radicals, molecular ions, Rydberg molecules, transition states, Van der Waals complexes, or systems of colliding atoms as in Bose-Einstein condensates. A peculiar use of the term molecular is as a synonym to covalent, which arises from the fact that, unlike molecular covalent compounds, ionic compounds do not yield well-defined smallest particles that would be consistent with the definition above. No typical "smallest particle" can be defined for covalent crystals, or network solids, which are composed of repeating unit cells that extend indefinitely either in a plane (such as in graphite) or three-dimensionally (such as in diamond). Although the concept of molecules was first introduced in 1811 by Avogadro, and was accepted by many chemists as a result of Dalton's laws of Definite and Multiple Proportions (1803-1808), with notable exceptions (Boltzmann, Maxwell, Gibbs), the existence of molecules as anything other than convenient mathematical constructs was still an open debate in the physics community until the work of Perrin (1911), and was strenuously resisted by early positvists such as Mach. The modern theory of molecules makes great use of the many numerical techniques offered by computational chemistry. Dozens of molecules have now been identified in interstellar space by microwave spectroscopy. microwave spectroscopy (right) representations of the terpenoid, atisane. In the 3D model on the left, carbon atoms are represented by gray spheres; white spheres represent the hydrogen atoms and the cylinders represent the bonds. The model is enveloped in a "mesh" representation of the molecular surface, colored by areas of positive (red) and negative (blue) electric charge. In the 3D model (center), the light-blue spheres represent carbon atoms, the white spheres are hydrogen atoms, and the cylinders in between the atoms correspond to single bonds.]]

Chemical bond

:See main article chemical bond In a molecule, the atoms are joined by shared pairs of electrons in a chemical bond. It may consist of atoms of the same chemical element, as with oxygen (O₂), or of different elements, as with water (H₂O).

Size

Most molecules are much too small to be seen with the naked eye, but there are exceptions. DNA, a macromolecule, can reach macroscopic sizes. The smallest molecule is the hydrogen molecule. The interatomic distance is 0.15 nanometres (1.5 Å). But the size of its electron cloud is difficult to define precisely. Under standard conditions molecules have a dimension of a few to a few dozen Å.

Empirical formula

:See main article empirical formula The empirical formula of a molecule is the simplest integer ratio of the chemical elements that constitute the compound. For example, in their pure forms, water is always composed of a 2:1 ratio of hydrogen to oxygen, and ethyl alcohol or ethanol is always composed of carbon, hydrogen, and oxygen in a 2:6:1 ratio. However, this does not determine the kind of molecule uniquely - dimethyl ether has the same ratio as ethanol, for instance. Molecules with the same atoms in different arrangements are called isomers. The empirical formula is often the same as the molecular formula but not always. For example the molecule acetylene has molecular formula C2H2, but the simplest integer ratio of elements is CH.

Chemical formula

:See main article chemical formula The chemical formula reflects the exact number of atoms that compose a molecule. The molecular mass can be calculated from the chemical formula and is expressed in conventional units equal to 1/12 from the mass of a ¹²C isotope atom. For network solids, the term formula unit is used in stoichiometric calculations.

Molecular geometry

:See main article molecular geometry Molecules have fixed equilibrium geometries—bond lengths and angles—. A pure substance is composed of molecules with the same geometrical structure. The chemical formula and the structure of a molecule are the two important factors that determine its properties, particularly its reactivity. Isomers share a chemical formula but normally have very different properties because of their different structures. Stereoisomers, a particular type of isomers, may have very similar physico-chemical properties and at the same time very different biochemical activities.

Molecular spectroscopy

:See main article spectroscopy Molecular spectroscopy is the study of the response (spectrum) of a molecule to a signal of known energy (or frequency, according to Planck's formula). This signal is usually an electromagnetic wave or a beam of electrons, but new molecular spectroscopies, such as the positron spectroscopy, are under development. The molecular response can be signal absorption (absorption spectroscopy), emission of another signal (emission spectroscopy), fragmentation, or a change in its chemical nature. Spectroscopy is recognized as the most powerful tool in the investigation of the microscopic properties of molecules, and, in particular, their energy levels. Nowadays, in order to extract the maximum microscopic information from the experimental results, spectroscopical studies are very often coupled with computational chemical investigations. The theoretical background of spectroscopy is the scattering theory.

Repeating unit

In polymer chemistry, a structural unit is a building block of a polymer chain. It is the result of a monomer residue which has been polymerized. Contrast this with repeating unit, which is the shortest sequence that can be found repeatedly in a polymer. This distinction is necessary in order to estimate the molecular weight of polymers correctly. Consider this example: Take polyethylene terephthalate. The monomers which could be used to create this polymer are ethylene glycol and terephthalic acid: HO-CH₂-CH₂-OH and HOOC-Ph-COOH In the polymer, there are two structural units, which look like -O-CH₂-CH₂-O- and -CO-PH-CO- The repeating unit looks like -CH₂-CH₂-O-CO-Ph-CO-O-

Monomer

In chemistry, a monomer (from Greek mono "one" and meros "part") is a small molecule that may become chemically bonded to other monomers to form a polymer. Examples of monomers are hydrocarbons such as the alkene and arene (homologous) series. Here hydrocarbon monomers such as styrene and ethene form polymers used as plastics like polystyrene and polyethene. In addition, Lipids are formed from monomers of fatty acids and glycerol. Amino acids are natural monomers, and polymerize to form proteins. Glucose monomers can also polymerize to form starches, amylopectins and glycogen polymers. In this case the polymerization reaction is known as a dehydration or condensation reaction (due to the formation of water (H₂O) as one of the products) where a hydrogen atom and a hydroxyl (-OH) group are lost to form H₂O and an oxygen molecule bonds between each monomer unit. Note that the lower molecular weight compounds built from monomers are also referred to as dimers, trimers, tetramers, pentamers, octamers, 20-mers, etc. if they have 2, 3, 4, 5, 8, or 20 monomer units, respectively. Any number of these monomer units may be indicated by the appropriate prefix, eg, decamer, being a 10-unit monomer chain or polymer. Larger numbers are often stated in English in lieu of Greek. Polymers with relatively low number of units are called oligomers. See also:
- Oligomer
- Polymer
- Polymerization
- Important publications in polymer chemistry Category:Polymer chemistry ko:단위체 ja:モノマー

Chemical reaction

A chemical reaction is a process that results in the interconversion of chemical substances . The substance(s) initially involved in a chemical reaction are called reactants. Chemical reactions are characterized by a chemical change and it yields one or more product(s) which are different from the reactants. Classically, chemical reactions encompass changes that strictly involve the motion of electrons in the forming and breaking of chemical bonds, although the general concept of a chemical reaction, in particular the notion of a chemical equation, is applicable to transformations of elementary particles, as well as nuclear reactions. Many different chemical reactions are used in combinations in chemical synthesis in order to get a desired product. In biochemistry, series of chemical reactions form metabolic pathways, since straight synthesis of a product would be energetically impossible in conditions within a cell. Chemical reactions are also divided into organic reactions and inorganic reactions.

Reaction types

There are five major classifications of chemical reactions. Some common and widely used terms are:
- Isomerization in which a chemical compound undergoes a structural rearrangement without any change in its net atomic composition; see stereoisomerism
- Direct combination or synthesis, in which two or more chemical element or compounds unite to form a more complex product; f.e. formation of water from hydrogen and oxygen
- Chemical decomposition or analysis, in which a compound is decomposed into smaller compounds; f.e. combustion of hydrocarbons
- Single displacement or substitution, characterized by an element being displaced out of a compound by a more reactive element; f.e. acid-base reactions
- Double displacement or coupling substitution , in which two compounds in aqueous solution (usually ionic) exchange elements or ions to form different compounds. Some branches of chemistry include any minor changes in chemical conformation in the reaction types, while others consider these changes merely as physical properties of a compound. The collision of more than two particles into the ordered structure necessary to perform chemical transformations is extremely unlikely; which is why ternary reactions in practice are not observed. A chemical reaction may require three or more reagents, but the process can generally be decomposed into a stepwise series or a set of stepwise reactions of the above. The large diversity of chemical reactions makes it difficult to establish simple criteria for functional (as opposed to mechanistic) classification. However, some kinds of reactions have similarities which make it possible to define some larger groups. A few examples are:
- Organic reactions, which encompass several different kinds of reactions involving compounds which have carbon as the main element in their molecular structure. These reactions occur mostly according to, within, by, or via functional groups. Reactions in petrochemistry aren't always classified as organic.
- Redox reactions, which involve augmenting or decreasing the electrons associated with a particular atom. according to its oxidation number.
- Combustion, where a substance reacts with oxygen gas;

Thermochemistry

See main article: Thermochemistry. Thermochemistry deciphers whether a specific chemical reaction can or cannot occur. Thermodynamics (or what is now known as equilibrium thermodynamics) understands the reaction in terms of the initial and final states of the reaction mixture. Reactions very seldom occur directly. Usually, reactants must collide to form an activated complex. This complex has a higher internal energy than the original reactants combined, having gained some from the kinetic energy of the reactant substances' collision. This energy allows for the rearrangement of bonds which constitutes the reaction. In some reactions, the reactants may pass through several reactive intermediates before becoming products. Thermodynamics does not attempt to figure out the process by which a reaction occurs. This field of study is taken up by the field of chemical kinetics. Another question "How fast is the reaction?" is also left completely unanswered by it. Chemical kinetics attempts to put all these phenomena into perspective.

Chemical equilibrium

Every chemical reaction is, in theory, reversible. In a forward reaction the substances defined as reactants are converted to products. In a reverse reaction products are converted into reactants. Chemical equilibrium is the state in which the forward and reverse reaction rates are equal, thus preserving the amount of reactants and products. However, a reaction in equilibrium can be driven in the forward or reverse direction. This is done by changing the reaction conditions such as temperature or pressure. Le Chatelier's principle can be used to predict whether products or reactants will be formed. Although all reactions are reversible to some extent, some reactions can be classified as irreversible. An irreversible reaction is one that "goes to completion." This phrase means that nearly all of the reactants are used to form products. These reactions are very difficult to reverse even under extreme conditions.

Exothermic reactions

Le Chatelier's principle According to energy balance criteria, that is, chemical reaction equilibria criteria, any closed system will tend to minimize its free energy. Without any outside influence, any reaction mixture, too, will try to do the same. For many cases, an analysis of the enthalpy of the system will give a decent account of the energetics of the reaction mixture. The enthalpy of a reaction is calculated using standard reaction enthalpies and the Hess' law of constant heat summation. Many of these enthalpies may be found in beginners' books on thermodynamics. For example, consider the combustion of methane in oxygen: :CH₄ + 2 O₂ → CO₂ + 2 H₂O By calculating the amounts of energy required to break all the bonds on the left ("before") and right ("after") sides of the equation using collected data, it is possible to calculate the energy difference between the reactants and the products. This is referred to as ΔH, where Δ (Delta) means difference, and H stands for enthalpy, a measure of energy which is equal to the heat transferred at constant pressure. ΔH is usually given in units of kilojoules (kJ) or in kilocalories (kcal). If ΔH is negative for the reaction, then energy has been released often in the form of heat. This type of reaction is referred to as an exothermic reaction (literally, outside heat, or throwing off heat). An exothermic reaction is more favourable and thus more likely to occur. An example reaction is combustion, known from everyday experience, since burning gas in air produces heat.

Endothermic reactions

combustion A reaction may have a positive ΔH. If a reaction has a positive ΔH, it consumes energy as the reaction moves towards completion. This type of reaction is called an endothermic reaction (literally, inside heat, or absorbing heat). The above rule, "Exothermic reactions are favourable", is usually true. However, there may be situations where exothermic reactions may not be favourable. This happens when the stability obtained due to loss of enthalpy is off set by a corresponding decrease in entropy (a measure of disorder). The exact rule is that a reaction is favourable when the Gibbs free energy of that reaction is negative where ΔG = ΔH − TΔS; ΔG being the change in Gibbs free energy, ΔH being the change in enthalpy, and ΔS is the change in entropy A reaction is called spontaneous if its thermodynamically favoured, by that meaning that it causes a net increase on entropy. Spontaneous reactions (in opposition to non-spontaneous reactions) do not need external perturbations (such as energy supplement) to happen. In a system at chemical equilibrium, it is expected to have larger concentrations of the substances formed by the spontaneous direction of the process. Thus, in a global isolated system (which it strictly isn't, see entropy), spontaneous reactions may be understood to occur without human interference. Most spontaneus reactions in this system are exothermic (such as rusting) or metamorphosis, thus increasing the global entropy, though photosynthesis is an important exeption (in a global system).

Chemical kinetics

See main article: Chemical kinetics. The rate of a chemical reaction is a measure of how the concentration of the involved substances changes with time. Analysis of reaction rates is important for several applications, such as in chemical engineering or in chemical equilibrium study. Rates of reaction depends basically on:
- Reactant concentrations, which usually make the reaction happen at a faster rate if raised,
- Surface Area, the amount of the substance being used,
- Pressure, By increasing the pressure, you squeeze the molecules together so you will increase the frequency of collisions between the molecules.
- Activation energy, which is defined as the amount of energy required to make the reaction start and carry on spontaneously. Higher activation energy implies that a reaction will be harder to start and, therefore, slower.
- Temperature, which hastens reactions if raised, because higher temperature means that the involved species will have more energy, thus making the reaction easier to happen,
- The presence or absence of a catalyst. Catalysts are substances which increases the speed of a reaction by lowering the activation energy needed for the reaction to take place. A catalyst is not destroyed or changed during a reaction, so it can be used again. Reaction rates are related to the concentrations of substances involved in reactions, as quantified by the law of mass action. Reactions whose rates are independent of reactant concentrations are called zero-order reactions.

External links

- [http://www.purchon.com/chemistry/rates.htm#surface Rate of reaction]

References

- IUPAC Gold Book [http://www.iupac.org/goldbook/C01033.pdf Definition]
- Category:Chemistry ko:화학 반응 ja:化学反応

Polymerization

Polymerization is a process of reacting monomer molecules together in a chemical reaction to form linear chains or a three-dimensional network of polymer chains ^[1]. There are many forms of polymerization and different systems exist to categorize them. The main categories are
- addition polymerization
- step-growth polymerization. It should be noted that there is no standard terminology in the literature to represent these types of polymerizations. Hence, there are multiple terms for the same type of polymerization. For example, "step polymerization", "step-growth polymerization" refer to the same type of polymerization.

Overview

Addition polymerization involves the linking together of molecules incorporating double or triple chemical bonds. These unsaturated monomers (the identical molecules which make up the polymers) have extra, internal, bonds which are able to break and link up with other monomers to form the repeating chain. Addition polymerization is involved in the manufacture of polymers such as polyethene, polypropylene and polyvinyl chloride (PVC). A special case of addition polymerization leads to living polymerization. Condensation polymerization occurs when monomers bond together through condensation reactions. Typically these reactions can be achieved through reacting molecules incorporating alcohol, amine or carboxylic acid (or other carboxyl derivative) functional groups. When an amine reacts with a carboxylic acid an amide or peptide bond is formed, with the release of water (hence condensation polymerization.) This is the process through which amino acids link up to form proteins, as well as how kevlar is formed. The chain growth-step growth system categorizes polymers based on their mechanism. While most polymers will fall into their similar category from the addition-condensation method of categorization, there are a few exceptions. Chain growth polymers are defined as polymers formed by the reaction of monomer with a reactive center. These polymers grow to high molecular weight at a very fast rate. It is important to note that the overall conversion rates between chain and step growth polymers are similar, but that high molecular weight polymers are formed in addition reactions much more quickly than with step polymerizations. Step growth polymers are defined as polymers formed by the stepwise reaction between functional groups of monomer. Most step growth polymers are also classified as condensation polymers, but not all step growth polymers (like polyurethanes formed from isocyanate and alcohol bifunctional monomers) release condensates. Step growth polymers increase in molecular weight at a very slow rate at lower conversions and only reach moderately high molecular weights at very high conversion (i.e. >95%). To alleviate inconsistencies in these naming methods, adjusted definitions for condensation and addition polymers have been developed. A condensation polymer is defined as a polymer that involves elimination of small molecules during its synthesis, or contains functional groups as part of its backbone chain, or its repeat unit does not contain all the atoms present in the hypothetical monomer to which it can be degraded. Addition polymerization involves the breaking of double or triple bonds, which are used to link monomers into chains. In the polymerization of ethene (fig. 1), its pi bond is broken and these two electrons rearrange to create a new propagating center like the one that attacked it. The form this propagating center takes depends on the specific type of addition mechanism. There are several mechanisms through which this can be initiated. The free radical mechanism was one of the first methods to be used. Free radicals are very reactive atoms or molecules which have unpaired electrons. Taking the polymerization of ethene as an example, the free radical mechanism can be divided in to three stages: initiation, propagation and termination. right Initiation is the creation of free radicals necessary for propagation. The radicals can be created from radical initiators, such as organic peroxide molecules, molecules containing an O-O single bond, by reacting oxygen with ethene. The products formed are unstable and easily break down into two radicals. In an ethene monomer, one electron pair is held securely between the two carbons in a sigma bond. The other is more loosely held in a pi bond. The free radical uses one electron from the pi bond to form a more stable bond with the carbon atom. The other electron returns to the second carbon atom, turning the whole molecule in to another radical. Propagation is the rapid reaction of this radicalised ethene molecule with another ethene monomer, and the subsequent repetition to create the repeating chain. Termination occurs when a radical reacts in a way that prevents further propagation. The most common method of termination is by coupling where two radical species react with each other forming a single molecule. Another, less common method of termination is disproportionation where two radicals meet, but instead of coupling, they exchange a proton, which gives two terminated chains, one saturated and the other with a terminal double bond. Free radical addition polymerization of ethylene must take place at high temperatures and pressures, approximately 300°C and 2000 At. While most other free radical polymerizations do not require such extreme temperatures and pressures, they do tend to lack control. One effect of this lack of control is a high degree of branching. Also, as termination occurs randomly, when two chains collide, it is impossible to control the length of individual chains. A newer method of polymerization similar to free radical, but allowing more control involves the Ziegler-Natta catalyst. The problem of branching occurs during propagation, when a chain curls back on itself and breaks - leaving irregular chains sprouting from the main carbon backbone. Branching makes the polymers less dense and results in low tensile strength and melting points. Developed by Karl Ziegler and Giulio Natta in the 1950s, Ziegler-Natta catalysts (triethylaluminium in the presence of a metal(IV) chloride) largely solved this problem. Instead of a free radical reaction, the initial ethene monomer inserts between the aluminium atom and one of the ethyl groups in the catalyst. The polymer is then able to grow out from the aluminium atom and results in almost totally unbranched chains. With the new catalysts, the tacticity of the polypropene chain, the alignment of alkyl groups, was also able to be controlled. Different metal chlorides allowed the selective production of each form i.e., syndiotactic, isotactic and atactic polymer chains could be selectively created. However there were further complications to be solved. If the Ziegler-Natta catalyst was poisoned or damaged then the chain stopped growing. Also, Ziegler-Natta monomers have to be small, and it was still impossible to control the molecular mass of the polymer chains. Again new catalysts, the metallocenes, were developed to tackle these problems. Due to their structure they have less premature chain termination and branching. Other forms of addition polymerization include cationic and anionic polymerization. While not used to a large extent in industry yet due to stringent reaction conditions such as lack of water and oxygen, these methods provide ways to polymerize some monomers that cannot be polymerized by free radical methods such as polypropylene. Cationic and anionic mechanisms are also more ideally suited for living polymerizations, although free radical living polymerizations have also been developed.

History

Polymerization dates back to the beginning of DNA based life, as both DNA and proteins can be considered polymers. The first 'synthetic' polymers of the 19th century were actually formed by modifying natural polymers. For example nitrocellulose was manufactured by reacting cellulose with nitric acid. The first genuinely man-made polymer, the phenol-formaldehyde resin bakelite, was synthesized in 1872. However, research into polymers and polymerization only really accelerated in the 1930s after the serendipitous discovery of polyethene by the chemical company ICI.

References

- ^[1] Introduction to Polymers 1987 R.J. Young Chapman & Hall ISBN 0-412-22170-5 Category:Chemical processes Category:Polymer chemistry Category:Polymers Category:Chemical reactions ja:重合反応

Protein

. This protein was the first to have its structure solved by X-ray crystallography by Max Perutz and Sir John Cowdery Kendrew in 1958, which led to them receiving a Nobel Prize in Chemistry.]] A protein (in Greek πρωτεϊνη = first thread) is a complex, high-molecular-weight organic compound that consists of amino acids joined by peptide bonds. Proteins are essential to the structure and function of all living cells and viruses. Many proteins are enzymes or subunits of enzymes. Other proteins play structural or mechanical roles, such as those that form the struts and joints of the cytoskeleton, serving as biological scaffolds for the mechanical integrity and tissue signalling functions. Still more functions filled by proteins include immune response and the storage and transport of various ligands. In nutrition, proteins serve as the source of amino acids for organisms that do not synthesize those amino acids natively. Proteins are one of the classes of bio-macromolecules, alongside polysaccharides, lipids, and nucleic acids, that make up the primary constituents of living things. They are among the most actively-studied molecules in biochemistry, and were discovered by Jöns Jakob Berzelius in 1838. Almost all natural proteins are encoded by DNA. DNA is transcribed to yield RNA, which serves as a template for translation by ribosomes.

Properties of Protein

Structure

ribosome Main article: Protein structure Proteins are amino acid chains that fold into unique 3-dimensional structures. The shape into which a protein naturally folds is known as its native state, which is determined by its sequence of amino acids. Thus, proteins are their own polymers, with amino acids being the monomers. Biochemists refer to four distinct aspects of a protein's structure:
- Primary structure: the amino acid sequence
- Secondary structure: highly patterned sub-structures—alpha helix and beta sheet—or segments of chain that assume no stable shape. Secondary structures are locally defined, meaning that there can be many different secondary motifs present in one single protein molecule.
- Tertiary structure: the overall shape of a single protein molecule; the spatial relationship of the secondary structural motifs to one another
- Quaternary structure: the shape or structure that results from the union of more than one protein molecule, usually called subunit proteins subunits in this context, which function as part of the larger assembly or protein complex. In addition to these levels of structure, proteins may shift between several similar structures in performing their biological function. In the context of these functional rearrangements, these tertiary or quaternary structures are usually referred to as "conformations," and transitions between them are called conformational changes. Proteins are separated into two groups: Complete and Incomplete. Incomplete proteins are from plants and do not include all 20 amino acids. Complete proteins come from an animal and include all 20 amino acids. You get protein from mostly everything you eat, but whether all the amino acids are in them depends on what the substance is. The primary structure is held together by covalent peptide bonds, which are made during the process of translation. The secondary structures are held together by hydrogen bonds. The tertiary structure is held together primarily by hydrophobic interactions but hydrogen bonds, ionic interactions, and disulfide bonds are usually involved too. The process by which the higher structures form is called protein folding and is a consequence of the primary structure. The mechanism of protein folding is not entirely understood. Although any unique polypeptide may have more than one stable folded conformation, each conformation has its own biological activity and only one conformation is considered to be the active, or native conformation. The two ends of the amino acid chain are referred to as the carboxy terminus (C-terminus) and the amino terminus (N-terminus) based on the nature of the free group on each extremity.

Working with proteins

Proteins are sensitive to their environment. They may only be active in their native state, over a small pH range, and under solution conditions with a minimum quantity of electrolytes. A protein in its native state is often described as folded. A protein that is not in its native state is said to be denatured. Denatured proteins generally have no well-defined secondary structure. Many proteins denature and will not remain in solution in distilled water. One of the more striking discoveries of the 20th century was that the native and denatured states in many proteins were interconvertible, that by careful control of solution conditions (by for example, dialyzing away a denaturing chemical), a denatured protein could be converted to native form. The issue of how proteins arrive at their native state is an important area of biochemical study, called the study of protein folding. Through genetic engineering, researchers can alter the sequence and hence the structure, "targeting", susceptibility to regulation and other properties of a protein. The genetic sequences of different proteins may be spliced together to create "chimeric" proteins that possess properties of both. This form of tinkering represents one of the chief tools of cell and molecular biologists to change and to probe the workings of cells. Another area of protein research attempts to engineer proteins with entirely new properties or functions, a field known as protein engineering. Protein-protein interactions can be screened for using two-hybrid screening.

Protein regulation

Various molecules and ions are able to bind to specific sites on proteins. These sites are called binding sites. They exhibit chemical specificity. The particle that binds is called a ligand. The strength of ligand-protein binding is a property of the binding site known as affinity. Since proteins are involved in practically every function performed by a cell, the mechanisms for controlling these functions therefore depend on controlling protein activity. Regulation can involve a protein's shape or concentration. Some forms of regulation include:
- Allosteric modulation: When the binding of a ligand at one site on a protein affects the binding of ligand at another site.
- Covalent modulation: When the covalent modification of a protein affects the binding of a ligand or some other aspect of the protein's function.

Diversity

Proteins are generally large molecules, having molecular masses of up to 3,000,000 (the muscle protein titin has a single amino acid chain 27,000 subunits long). Such long chains of amino acids are almost universally referred to as proteins, but shorter strings of amino acids are referred to as "polypeptides," "peptides" or rarely, "oligopeptides". The dividing line is undefined, though "polypeptide" usually refers to an amino acid chain lacking tertiary structure which may be more likely to act as a hormone (like insulin), rather than as an enzyme (which depends on its defined tertiary structure for functionality). Proteins are generally classified as soluble, filamentous or membrane-associated (see integral membrane protein). Nearly all the biological catalysts known as enzymes are soluble proteins (with a recent notable execption being the discovery of ribozymes, RNA molecules with the catalytic properties of enzymes.) Antibodies, the basis of the adaptive immune system, are another example of soluble proteins. Membrane-associated proteins include exchangers and ion channels, which move their substrates from place to place but do not change them; receptors, which do not modify their substrates but may simply shift shape upon binding them. Filamentous proteins make up the cytoskeleton of cells and much of the structure of animals: examples include tubulin, actin, collagen and keratin, all of which are important components of skin, hair, and cartilage. Another special class of proteins consists of motor proteins such as myosin, kinesin, and dynein. These proteins are "molecular motors," generating physical force which can move organelles, cells, and entire muscles. muscle

Role of Protein

Functions

Proteins are involved in practically every function performed by a cell, including regulation of cellular functions such as signal transduction and metabolism. For example, protein catabolism requires enzymes termed proteases and other enzymes such as glycosidases.

Within Nutrition

Protein is an important macronutrient to the human diet, supplying the body's needs for nitrogen and amino acids, the building blocks of proteins. The exact amount of dietary protein needed to satisfy these requirements may vary widely depending on age, sex, level of physical activity, and medical condition, as well as the RDA specified by the state. The recommended intake of protein differs from country to country, but it is marginalised between 0.8 and 1.2g / kg b.w (Per kilogram of bodyweight), however , in more serious athletes, requiring strength, the figure is somewhat between 1.0 and 2.0g per kilogram of Body weight, which is referred to as the maximum protein intake:benefits ratio. Although proteins are found in all foods, be it only in small amounts , protein is still well concentrated in foods such as legumes, nuts, and dairy products, the majority of which are protein choices for vegetarians. Protein is the major component in the regulation, growth and differentation of muscles, tendons, enzymes, skin, hair, eyes, as well as a tremendous variety of other organs and processes. The quality of protein intake is particularly important because different proteins supply essential amino acids in different proportions. Given an adequate intake of nitrogen, the human body can manufacture 10 of the 18 amino acids from glucose. The remaining 8 amino acids (threonine, valine, tryptophan, isoleucine, leucine, lysine, phenylalanine, and methionine) cannot be manufactured by the body and must be acquired through supplementation. Thus, they are termed essential amino acids. For use within the body, the majority of protein taken from food consumed is converted by protein catabolism into ammonia which, due to its toxicity, must be converted to either urea or uric acid,or in some animals is excreted in urine. Proteins possessing equal proportions of all essential amino acids in relatively abundant quantities are often termed "complete", or "High-Quality" Proteins, which are generally obtained from animal proteins, such as meat , and are rated using PDCAAS (Protein Digestibility Corrected Amino Acid Score). Despite what the name suggests, quality proteins are not essential for good supplementation or nutrition within the average person, however, the difference between amino acids in plant and animal proteins is discernable, particularly for athletes or bodybuilders as plant proteins lack two major amino acids found in animal proteins; lysine within grains, and methionine within legumes, major benefactors to a major athlete's dietary regime. Neverthelss, in terms of quality, amino acids found in plant and animal extracts are identical. Protein deficiency can lead to symptoms such as fatigue, insulin resistance, hair loss, loss of hair pigment, loss of muscle mass , low body temperature, hormonal irregularities, as well as loss of skin elsaticity . Severe protein deficiency, encountered only in times of famine, is fatal, due to the lack of material for the body to facilitate as energy. It has been known that in some "wild diets", in which people lose mass amounts of weight in a short period of time are attributed to deficiencies in protein, and thus loss in muscle mass, and not fat, which is widely known as a dangerous practice, particularly because of the benefits of muscle mass over fat. Excessive protein intake has also been linked to several problems;
- overreaction within the immune system
- liver dysfunction due to increased toxic residues
- loss of bone density, frailty of bones due to increased acidity in the blood and foundering (foot problems) in horses. It is assumed by reasearchers on the field, that excessive intake of protein forced increased calcium excretion. If there is to be excessive intake of protein, it is thought that a regular intake of calcium would be able to stablilise, or even increase the uptake of calcium by the small intestine, which would be more beneficial in older women . Proteins are often progenitors in allergies and allergic reactions to certain foods. This is because the structure of each form of protein is slightly different; some may trigger a response from the immune system while others remain perfectly safe. Many people are allergic to casein, the protein in milk; gluten, the protein in wheat and other grains; the particular proteins found in peanuts; or those in shellfish or other seafoods. It is extremely unusual for the same person to adversely react to more than two different types of proteins, due to the diversity between protein or amino acid types.

History

The first mention of the word protein, which means of first rank, were from a letter sent by Jöns Jakob "Jinglehimer Schmidt" Berzelius to Gerhardus Johannes Mulder on 10. July 1838, where he wrote: :«Le nom protéine que je vous propose pour l’oxyde organique de la fibrine et de l’albumine, je voulais le dériver de πρωτειοξ, parce qu’il paraît être la substance primitive ou principale de la nutrition animale.» Translated as: :"The name protein that I propose for the organic oxide of fibrin and albumin, I wanted to derive from [the Greek word] πρωτειοξ, because it appears to be the primitive or principal substance of animal nutrition." Investigation of proteins and their properties had been going on since about 1800 when scientists were finding the first signs of this, at the time, unknown class of organic compounds.

References

# Kerstetter, J. E., O'Brien, K. O., Insogna, K. L. (2003) "[http://www.ajcn.org/cgi/content/full/78/3/584S Dietary protein, calcium metabolism, and skeletal homeostasis revisited]" . J Clin Endocrinol Metab Vol 78, p584S-592S. # Kerstetter, J. E., O'Brien, K. O., Caseria, D.M, Wall, D. E. & Insogna, K. L (2005) "The impact of dietary protein on calcium absorption and kinetic measures of bone turnover in women" . J Clin Endocrinol Metab (2005) Vol 90, p26-31, . # Devine, A., Dick, I. M,, Islam I. M., Dhaliwal, S. S. & Prince, R. L. (2005) "Protein consumption is an important predictor of lower limb bone mass in elderly women" . Am J Clin Nutr (2005) volume 81 pages 423-428, . # Jeukendrup, A. & Gleeson, M. (2004) Sport Nutrition - An Introduction to Energy Production and Performance USA : Human Kinetics # Bean, A. (2004) Sport Nutrition for Serious Athletes London : Routledge

External links

- [http://www.expasy.uniprot.org UniProt the Universal Protein Resource]
- [http://www.proteinatlas.org Human Protein Atlas]
- [http://www.ihop-net.org/UniPub/iHOP/ iHOP - Information Hyperlinked over Proteins]
- [http://www.biochemweb.org/proteins.shtml Proteins: Biogenesis to Degradation - The Virtual Library of Biochemistry and Cell Biology]
- [http://web.mit.edu/lms/www/ MIT's Laboratory for Protein Molecular Self-Assembly]
- [http://www.puramatrix.com/pubs Numerous publications on synthetic biomimetic protein-based biomaterials]
- [http://www.westernblotting.org Protein Research: Western Blot Protocols, Troubleshooting and Theory]
- [http://www.rcsb.org The Protein Databank: The single worldwide repository for the processing and distribution of 3-D biological macromolecular structure data.]
- [http://web.indstate.edu/thcme/mwking/amino-acid-metabolism.html Amino acid metabolism]
- [http://www.biochem.szote.u-szeged.hu/astrojan/protein2.htm Protein Images] Category:Molecular biology Category:Biochemistry Category:Nutrition zh-min-nan:Nn̄g-pe̍h-chit ko:단백질 ja:蛋白質 simple:Protein th:โปรตีน

Biology

Biology is the study, or science, of life. It is concerned with the characteristics and behaviors of organisms, how species and individuals come into existence, and the interactions they have with each other and with the environment. Biology encompasses a broad spectrum of academic fields that are often viewed as independent disciplines. However, together they address the phenomenon of life over a wide range of scales. At the atomic and molecular scale, life is studied in the disciplines of molecular biology, biochemistry, and molecular genetics. At the level of the cell, it is studied in cell biology, and at multicellular scales, it is examined in physiology, anatomy, and histology. Developmental biology studies life at the level of an individual organism's development or ontogeny. Moving up the scale towards more than one organism, genetics considers how heredity works between parent and offspring. Ethology considers group behavior of more than one individual. Population genetics looks at the level of an entire population, and systematics considers the multi-species scale of lineages. Interdependent populations and their habitats are examined in ecology and evolutionary biology. A speculative new field is astrobiology (or xenobiology), which examines the possibility of life beyond the Earth.

Biology studies the variety of life (clockwise from top-left) E. coli, tree fern, gazelle, Goliath beetle

Principles of biology

Unlike physics, biology does not usually describe systems in terms of objects which obey immutable physical laws described by mathematics. Nevertheless, the biological sciences are characterized and unified by several major underlying principles and concepts: universality, evolution, diversity, continuity, homeostasis, and interactions.

Universality: Biochemistry, cells, and the genetic code

mathematics]] Main articles: Life The most salient example of biological universality is that all living things share a common carbon-based biochemistry and in particular pass on their characteristics via genetic material, which is based on nucleic acids such as DNA and which uses a common genetic code with only minor variations. Another universal principle is that all organisms (that is, all forms of life on Earth except for viruses) are made of cells. Similarly, all organisms share common developmental processes. For example, in most metazoan organisms, the basic stages of early embryonic development share similar morphological characteristics and include similar genes.

Evolution: The central principle of biology

Main article: Evolution The central organizing concept in biology is that all life has a common origin and has changed and developed through the process of evolution (see Common descent). This has led to the striking similarity of units and processes discussed in the previous section. Charles Darwin established evolution as a viable theory by articulating its driving force, natural selection (Alfred Russell Wallace is recognized as the co-discoverer of this concept). Genetic drift was embraced as an additional mechanism of evolutionary development in the modern synthesis of the theory. The evolutionary history of a species— which describes the characteristics of the various species from which it descended— together with its genealogical relationship to every other species is called its phylogeny. Widely varied approaches to biology generate information about phylogeny. These include the comparisons of DNA sequences conducted within molecular biology or genomics, and comparisons of fossils or other records of ancient organisms in paleontology. Biologists organize and analyze evolutionary relationships through various methods, including phylogenetics, phenetics, and cladistics (The major events in the evolution of life, as biologists currently understand them, are summarized on this evolutionary timeline).

Diversity: The variety of living organisms

evolutionary timeline, based on rRNA gene data, showing the separation of the three domains bacteria, archaea, and eukaryotes as described initially by Carl Woese. Trees constructed with other genes are generally similar, although they may place some early-branching groups very differently, presumably owing to rapid rRNA evolution. The exact relationships of the three domains are still being debated.]] Despite its underlying unity, life exhibits an astonishingly wide diversity in morphology, behavior, and life histories. In order to grapple with this diversity, biologists attempt to classify all living things. Scientific classification seeks to reflect the evolutionary trees (phylogenetic trees) of the organism being classified. Classification is the province of the disciplines of systematics and taxonomy. Taxonomy places organisms in groups called taxa, while systematics seeks to define their relationships with each other. This clasification technique has evolved to reflect advances in cladistics and genetics, shifting the focus from physical similarities and shared characteristics to phylogenetics. Traditionally, living things have been divided into five kingdoms: :Monera -- Protista -- Fungi -- Plantae -- Animalia However, many scientists now consider this five-kingdom system to be outdated. Modern alternative classification systems generally begin with the three-domain system: :Archaea (originally Archaebacteria) -- Bacteria (originally Eubacteria) -- Eukaryota These domains reflect whether the cells have nuclei or not, as well as differences in the cell exteriors. There is also a series of intracellular parasites that are progressively "less alive" in terms of metabolic activity: :Viruses -- Viroids -- Prions

Continuity: The common descent of life

Main article: Common descent Up into the 19th century, it was commonly believed that life forms could appear spontaneously under certain conditions (see abiogenesis). This misconception was challenged by William Harvey's diction that "all life [is] from [an] egg" (from the Latin "Omne vivum ex ovo"), a foundational concept of modern biology. It simply means that there is an unbroken continuity of life from its initial origin to the present time. A group of organisms is said to share a common descent if they share a common ancestor. All organisms on the Earth have been and are descended from a common ancestor or an ancestral gene pool. This last universal common ancestor of all organisms is believed to have appeared about 3.5 billion years ago. Biologists generally regard the universality of the genetic code as definitive evidence in favor of the theory of universal common descent (UCD) for all bacteria, archaea, and eukaryotes (see: origin of life).

Homeostasis: Adapting to change

Main article: Homeostasis Homeostasis is the ability of an open system to regulate its internal environment to maintain a stable condition by means of multiple dynamic equilibrium adjustments controlled by interrelated regulation mechanisms. All living organisms, whether unicellular or multicellular, exhibit homeostasis. Homeostasis manifests itself at the cellular level through the maintenance of a stable internal acidity (pH); at the organismic level, warm-blooded animals maintain a constant internal body temperature; and at the level of the ecosystem, as when atmospheric carbon dioxide levels rise and plants are theoretically able to grow healthier and remove more of the gas from the atmosphere. Tissues and organs can also maintain homeostasis.

Interactions: Groups and environments

organ of the genus Amphiprion that dwell among the tentacles of tropical sea anemones. The territorial fish protects the anemone from anemone-eating fish, and in turn the stinging tentacles of the anemone protects the anemone fish from its predators]] Every living thing interacts with other organisms and its environment. One reason that biological systems can be difficult to study is that so many different interactions with other organisms and the environment are possible, even on the smallest of scales. A microscopic bacterium responding to a local sugar gradient is responding to its environment as much as a lion is responding to its environment when it searches for food in the African savannah. For any given species, behaviors can be co-operative, aggressive, parasitic or symbiotic. Matters become more complex when two or more different species interact in an ecosystem. Studies of this type are the province of ecology.

Scope of biology

Main article: List of biology disciplines Biology has become such a vast research enterprise that it is not generally regarded as a single discipline, but as a number of clustered sub-disciplines. This article considers four broad groupings. The first group consists of those disciplines that study the basic structures of living systems: cells, genes etc.; the second group considers the operation of these structures at the level of tissues, organs, and bodies; the third group considers organisms and their histories; the final constellation of disciplines focuses on their interactions. It is important to note, however, that these boundaries, groupings, and descriptions are a simplified characterization of biological research. In reality, the boundaries between disciplines are fluid, and most disciplines frequently borrow techniques from each other. For example, evolutionary biology leans heavily on techniques from molecular biology to determine DNA sequences, which assist in understanding the genetic variation of a population; and physiology borrows extensively from cell biology in describing the function of organ systems.

Structure of life

DNA sequences and structures]] Main articles: Molecular biology, Cell biology, Genetics, Developmental biology Molecular biology is the study of biology at a molecular level. This field overlaps with other areas of biology, particularly with genetics and biochemistry. Molecular biology chiefly concerns itself with understanding the interactions between the various systems of a cell, including the interrelationship of DNA, RNA, and protein synthesis and learning how these interactions are regulated. Cell biology studies the physiological properties of cells, as well as their behaviors, interactions, and environment. This is done both on a microscopic and molecular level. Cell biology researches both single-celled organisms like bacteria and specialized cells in multicellular organisms like humans. Understanding cell composition and how they function is fundamental to all of the biological sciences. Appreciating the similarities and differences between cell types is particularly important in the fields of cell and molecular biology. These fundamental similarities and differences provide a unifying theme, allowing the principles learned from studying one cell type to be extrapolated and generalized to other cell types. Genetics is the science of genes, heredity, and the variation of organisms. In modern research, genetics provides important tools in the investigation of the function of a particular gene, or the analysis of genetic interactions. Within organisms, genetic information generally is carried in chromosomes, where it is represented in the chemical structure of particular DNA molecules. Genes encode the information necessary for synthesizing proteins, which in turn play a large role in influencing (though, in many instances, not completely determining) the final phenotype of the organism. Developmental biology studies the process by which organisms grow and develop. Originating in embryology, modern developmental biology studies the genetic control of cell growth, differentiation, and "morphogenesis," which is the process that gives rise to tissues, organs, and anatomy. Model organisms for developmental biology include the round worm Caenorhabditis elegans, the fruit fly Drosophila melanogaster, the zebrafish Brachydanio rerio, the mouse Mus musculus, and the weed Arabidopsis thaliana.

Physiology of organisms

Main articles: Physiology, Anatomy Physiology studies the mechanical, physical, and biochemical processes of living organisms by attempting to understand how all of the structures function as a whole. The theme of "structure to function" is central to biology. Physiological studies have traditionally been divided into plant physiology and animal physiology, but the principles of physiology are universal, no matter what particular organism is being studied. For example, what is learned about the physiology of yeast cells can also apply to human cells. The field of animal physiology extends the tools and methods of human physiology to non-human species. Plant physiology also borrows techniques from both fields. Anatomy is an important branch of physiology and considers how organ systems in animals, such as the nervous, immune, endocrine, respiratory, and circulatory systems, function and interact. The study of these systems is shared with medically oriented disciplines such as neurology and immunology.

Diversity and evolution of organisms

immunology of a population of organisms is sometimes depicted as if travelling on a fitness landscape. The arrows indicate the preferred flow of a population on the landscape, and the points A, B, and C are local optima. The red ball indicates a population that moves from a very low fitness value to the top of a peak]] Main articles: Evolutionary biology, Botany, Zoology Evolutionary biology is concerned with the origin and descent of species, as well as their change over time, and includes scientists from many taxonomically-oriented disciplines. For example, it generally involves scientists who have special training in particular organisms such as mammalogy, ornithology, or herpetology, but use those organisms as systems to answer general questions about evolution. Evolutionary biology also makes use of paleontologists, who use the fossil record to answer questions about the mode and tempo of evolution, as well as theoreticians in areas such as population genetics and evolutionary theory. In the 1990s, developmental biology re-entered evolutionary biology from its initial exclusion from the modern synthesis through the study of evolutionary developmental biology. Related fields which are often considered part of evolutionary biology are phylogenetics, systematics, and taxonomy. The two major traditional taxonomically-oriented disciplines are botany and zoology. Botany is the scientific study of plants. Botany covers a wide range of scientific disciplines that study the growth, reproduction, metabolism, development, diseases, and evolution of plant life. Zoology involves the study of animals, including the study of their physiology within the fields of anatomy and embryology. The common genetic and developmental mechanisms of animals and plants is studied in molecular biology, molecular genetics, and developmental biology. The ecology of animals is covered under behavioral ecology and other fields.

Classification of life

The dominant classification system is called Linnaean taxonomy, which includes ranks and binomial nomenclature. How organisms are named is governed by international agreements such as the International Code of Botanical Nomenclature (ICBN), the International Code of Zoological Nomenclature (ICZN), and the International Code of Nomenclature of Bacteria (ICNB). A fourth Draft BioCode was published in 1997 in an attempt to standardize naming in these three areas, but it has yet to be formally adopted. The International Code of Virus Classification and Nomenclature (ICVCN) remains outside the BioCode.

Interactions of organisms

International Code of Virus Classification and Nomenclature]] Main articles: Ecology, Ethology, Behavior, Biogeography Ecology studies the distribution and abundance of living organisms, and the interactions between organisms and their environment. The environment of an organism includes both its habitat, which can be described as the sum of local abiotic factors such as climate and geology, as well as the other the organisms that share its habitat. Ecological systems are studied at several different levels, from individuals and populations to ecosystems and the biosphere. As can be surmised, ecology is a science that draws on several disciplines. Ethology studies animal behavior (particularly of social animals such as primates and canids), and is sometimes considered a branch of zoology. Ethologists have been particularly concerned with the evolution of behavior and the understanding of behavior in terms of the theory of natural selection. In one sense, the first modern ethologist was Charles Darwin, whose book The expression of the emotions in animals and men influenced many ethologists. Biogeography studies the spatial distribution of organisms on the Earth, focusing on topics like plate tectonics, climate change, dispersal and migration, and cladistics.

History of the word "biology"

Formed by combining the Greek βίος (bios), meaning 'life', and λόγος (logos), meaning 'study of', the word "biology" in its modern sense seems to have been introduced independently by Gottfried Reinhold Treviranus (Biologie oder Philosophie der lebenden Natur, 1802) and by Jean-Baptiste Lamarck (Hydrogéologie, 1802). The word itself is sometimes said to have been coined in 1800 by Karl Friedrich Burdach, but it appears in the title of Volume 3 of Michael Christoph Hanov's Philosophiae naturalis sive physicae dogmaticae: Geologia, biologia, phytologia generalis et dendrologia, published in 1766.

History

Main articles: History of biology, History of medicine, History of genetics Major discoveries in biology include:
- Cell theory
- Germ theory of disease
- Genetics
- Evolution
- DNA

External links

- [http://www.rom.on.ca/biodiversity/biocode/biocode1997.html BioCode]: A proposal for organism naming.
- [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=Books NCBI Open-Access Books]
- PhyloCode, [http://www.ohiou.edu/phylocode/index.html]
- [http://tolweb.org/tree/phylogeny.html The Tree of Life]: A multi-authored, distributed Internet project containing information about phylogeny and biodiversity.
- [http://www.bioone.org/perlserv/?request=index-html BioOne] Bioscience research journals.
- [http://www.bionews.in/biologynews.htm Biology News] Biology News, Articles and Research discoversies.

Polymers

Physical properties of polymers

Branching

Stereoregularity

Constitution of polymers

Copolymers

Chemical properties of polymers

Intermolecular forces

Polymer characterization

External links

Molecule

Chemical bond

Size

Empirical formula

Chemical formula

Molecular geometry

Molecular spectroscopy

See also

Related lists

Repeating unit

Monomer

Chemical reaction

Reaction types

Thermochemistry

Chemical equilibrium

Exothermic reactions

Endothermic reactions

Chemical kinetics

See also

External links

References

Polymerization

Overview

History

See also

References

Protein

Properties of Protein

Structure

Working with proteins

Protein regulation

Diversity

Role of Protein

Functions

Within Nutrition

History

See also

References

External links

Biology

Principles of biology

Universality: Biochemistry, cells, and the genetic code

Evolution: The central principle of biology

Diversity: The variety of living organisms

Continuity: The common descent of life

Homeostasis: Adapting to change

Interactions: Groups and environments

Scope of biology

Structure of life

Physiology of organisms

Diversity and evolution of organisms

Classification of life

Interactions of organisms

History of the word "biology"

History

Related topics

External links

Further reading