Biomolecule

A representation of the 3D structure of myoglobin, showing coloured alpha helices. This protein was the first to have its structure solved by X-ray crystallography by Max Perutz and Sir John Cowdery Kendrew in 1958, for which they received a Nobel Prize in Chemistry.

A biomolecule is any organic molecule that is produced by a living organism, including large polymeric molecules such as proteins, polysaccharides, and nucleic acids as well as small molecules such as primary metabolites, secondary metabolites, and natural products.

As organic molecules, biomolecules consist primarily of carbon and hydrogen, nitrogen, and oxygen, and, to a smaller extent, phosphorus and sulfur. Other elements sometimes are incorporated but are much less common.

Contents

Types of biomolecules

A diverse range of biomolecules exist, including:

Nucleosides and nucleotides

Nucleosides are molecules formed by attaching a nucleobase to a ribose ring. Examples of these include cytidine, uridine, adenosine, guanosine, thymidine and inosine.

Nucleosides can be phosphorylated by specific kinases in the cell, producing nucleotides, which are the molecular building blocks of DNA (deoxyribonucleic acid) and RNA (ribonucleic acid). nucleotides contain carbon nitrogen oxygen hydrogen and phosphorus.they take part in energy transfer systemthis is a group of small complex molecules forming information transfer system in cell and are basic unit of nuclic acid each nucleotide is made of aacyclic nitrogen base a pentose and one to 3 phosphate group

Saccharides

Monosaccharides are the simplest form of carbohydrates with only one simple sugar. They essentially contain an aldehyde or ketone group in their structure. Examples of monosaccharides are the hexoses glucose, fructose, and galactose and pentoses, ribose, and deoxyribose

Disaccharides are formed when two monosaccharides, or two single simple sugars, form a bond with removal of water. Examples of disaccharides include sucrose, maltose, and lactose

Polysaccharides are polymerized monosaccharides, complex, carbohydrates. They have multiple simple sugars. Examples are starch, cellulose, and glycogen. They are generally large and often have a complex branched connectivity. Shorter polysaccharides, with 2 - 10 monomers, are called oligosaccharides.[1]

Lignin

Lignin is a random polymer composed mainly of aromatic rings with short (up to three) aliphatic carbons chains connecting the rings. Lignin is the second most common biopolymer (after cellulose) and is one of the primary structural components of most plants. It contains subunits derived from p-coumaryl alcohol, coniferyl alcohol, and sinapyl alcohol[2] and is unusual among biomolecules in that it is racemic i.e. it is not optically active. The lack of optical activity is because the polymerization of lignin occurs via free radical coupling reactions in which there is no preference for either configuration at a chiral center.

Lipids

Lipids are chiefly fatty acid esters, and are the basic building blocks of biological membranes. Another biological role is energy storage (e.g., triglycerides). Most lipids consist of a polar or hydrophilic head (typically glycerol) and one to three nonpolar or hydrophobic fatty acid tails, and therefore they are amphiphilic. Fatty acids consist of unbranched chains of carbon atoms that are connected by single bonds alone (saturated fatty acids) or by both single and double bonds (unsaturated fatty acids). The chains are usually 14-24 carbon groups long, but it is always an even number.

For lipids present in biological membranes, the hydrophilic head is from one of three classes:

Other lipids include prostaglandins and leukotrienes which are both 20-carbon fatty acyl units synthesized from arachidonic acid. They are also known as fatty acids

Amino acids

Amino acids contain both amino and carboxylic acid functional groups. (In biochemistry, the term amino acid is used when referring to those amino acids in which the amino and carboxylate functionalities are attached to the same carbon, plus proline which is not actually an amino acid).

Amino acids are the building blocks of long polymer chains. With 2-10 amino acids such chains are called peptides, with 10-100 they are often called polypeptides, and longer chains are known as proteins. These protein structures have many structural and enzymatic roles in organisms.

There are twenty amino acids that are encoded by the standard genetic code, but there are more than 500 natural amino acids. When amino acids other than the set of twenty are observed in proteins, this is usually the result of modification after translation (protein synthesis). Only two amino acids other than the standard twenty are known to be incorporated into proteins during translation, in certain organisms:

Besides those used in protein synthesis, other biologically important amino acids include carnitine (used in lipid transport within a cell), ornithine, GABA and taurine.

Protein structure

The particular series of amino acids that form a protein is known as that protein's primary structure. This sequence is determined by the genetic makeup of the individual. Proteins have several, well-classified, elements of local structure formed by intermolecular attraction, this forms the secondary structure of protein. They are broadly divided in two, alpha helix and beta sheet, also called beta pleated sheets. Alpha helices are formed of coiling of protein due to attraction between amine group of one amino acid with carboxylic acid group of other. The coil contains about 3.6 amino acids per turn and the alkyl group of amino acid lie outside the plane of coil. Beta pleated sheets are formed by strong continuous hydrogen bond over the length of protein chain. Bonding may be parallel or antiparallel in nature. Structurally, natural silk is formed of beta pleated sheets. Usually, a protein is formed by action of both these structures in variable ratios. Coiling may also be random. The overall 3D structure of a protein is termed its tertiary structure. It is formed as result of various forces like hydrogen bonding, disulphide bridges, hydrophobic interactions, hydrophilic interactions, van der Waals force etc. When two or more different polypeptide chains cluster to form a protein, quaternary structure of protein is formed. Quarternary structure is a unique attribute of polymeric and heteromeric proteins like haemoglobin, which consists of two alpha and two beta peptide chains.

Apoenzymes

An apoenzyme is the inactive storage and generally secretory form of a protein. This is required to protect the secretory cell from the activity of that protein. Apoenzymes becomes active enzyme on addition of a cofactor. Cofactors can be either inorganic (e.g., metal ions and iron-sulfur clusters) or organic compounds, (e.g., flavin and heme). Organic cofactors can be either prosthetic groups, which are tightly bound to an enzyme, or coenzymes, which are released from the enzyme's active site during the reaction.

Isoenzymes

Isoenzymes are the enzymes with similar function but different structure. they are products of different genes. They are produced in different organs to perform same function. LDH are examples of such enzymes. Their varied levels in blood are used to determine any deformity in the organ of secretion.

Vitamins

A vitamin is a compound that is generally not synthesized by a given organism but is nonetheless vital to its survival or health (for example coenzymes). These compounds must be absorbed, or eaten, but typically only in trace quantities. When originally proposed by Casimir Funk, a Polish biochemist, he believed them to all be basic and therefore named them vital amines. The "l" was later dropped to form the word vitamines.

See also

References

  1. ↑ Pigman, W.; D. Horton (1972). The Carbohydrates Vol. 1A. San Diego: Academic Press. pp. 3. ISBN 68-26647. 
  2. ↑ K. Freudenberg & A.C. Nash (eds) (1968). Constitution and Biosynthesis of Lignin. Berlin: Springer-Verlag.