Structural and functional constraints in the evolution of protein families

Item Type:	Review
Title:	Structural and functional constraints in the evolution of protein families
Creators Name:	Worth, C.L. and Gong, S. and Blundell, T.L.
Abstract:	High-throughput genomic sequencing has focused attention on understanding differences between species and between individuals. When this genetic variation affects protein sequences, the rate of amino acid substitution reflects both Darwinian selection for functionally advantageous mutations and selectively neutral evolution operating within the constraints of structure and function. During neutral evolution, whereby mutations accumulate by random drift, amino acid substitutions are constrained by factors such as the formation of intramolecular and intermolecular interactions and the accessibility to water or lipids surrounding the protein. These constraints arise from the need to conserve a specific architecture and to retain interactions that mediate functions in protein families and superfamilies.
Keywords:	Amino Acid Sequence, Amino Acid Substitution, Molecular Evolution, Hydrogen Bonding, Hydrophobic and Hydrophilic Interactions, Kinetics, Molecular Models, Molecular Sequence Data, Protein Binding, Protein Folding, Secondary Protein Structure, Proteins, Amino Acid Sequence Homology
Source:	Nature Reviews Molecular Cell Biology
ISSN:	1471-0072
Publisher:	Nature Publishing Group
Volume:	10
Number:	10
Page Range:	709-720
Date:	October 2009
Official Publication:	https://doi.org/10.1038/nrm2762
PubMed:	View item in PubMed

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