Fortier, Caleb (2012) Protein structure. Research World, Delhi, India. ISBN 9788132332084
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Abstract
Proteins are an important class of biological macromolecules present in all organisms. All proteins are polymers of amino acids. Classified by their physical size, proteins are nanoparticles (definition: 1-100 nm). Each protein polymer - also known as a polypeptide - consists of a sequence of 20 different L-a-amino acids, also referred to as residues. For chains under 40 residues the term peptide is frequently used instead of protein. To be able to perform their biological function, proteins fold into one or more specific spatial conformations, driven by a number of non-covalent interactions such as hydrogen bonding, ionic interactions, Van Der Waals forces, and hydrophobic packing. To understand the functions of proteins at a molecular level, it is often necessary to determine their three-dimensional structure. This is the topic of the scientific field of structural biology, which employs techniques such as X-ray crystallography, NMR spectroscopy, and dual polarization interferometry to determine the structure of proteins. Protein structures range in size from tens to several thousand residues. Very large aggregates can be formed from protein subunits: for example, many thousand actin molecules assemble into a microfilament. A protein may undergo reversible structural changes in performing its biological function. The alternative structures of the same protein are referred to as different conformations, and transitions between them are called conformational changes.
| Item Type: | Book |
|---|---|
| Subjects: | Q Science > QP Physiology |
| Divisions: | Electronic Books |
| Depositing User: | Esam @ Hisham Muhammad |
| Date Deposited: | 12 Feb 2023 06:46 |
| Last Modified: | 12 Feb 2023 06:46 |
| URI: | http://odlsystem2.utm.my/id/eprint/3966 |
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