Recurrent structural motifs in non-homologous protein structures.

Details

Serval ID
serval:BIB_FB91592FAE3A
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Recurrent structural motifs in non-homologous protein structures.
Journal
International journal of molecular sciences
Author(s)
Johansson M.U., Zoete V., Guex N.
ISSN
1422-0067 (Print)
ISSN-L
1422-0067
Publication state
Published
Issued date
10/04/2013
Peer-reviewed
Oui
Volume
14
Number
4
Pages
7795-7814
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: epublish
Abstract
We have extracted an extensive collection of recurrent structural motifs (RSMs), which consist of sequentially non-contiguous structural motifs (4-6 residues), each of which appears with very similar conformation in three or more mutually unrelated protein structures. We find that the proteins in our set are covered to a substantial extent by the recurrent non-contiguous structural motifs, especially the helix and strand regions. Computational alanine scanning calculations indicate that the average folding free energy changes upon alanine mutation for most types of non-alanine residues are higher for amino acids that are present in recurrent structural motifs than for amino acids that are not. The non-alanine amino acids that are most common in the recurrent structural motifs, i.e., phenylalanine, isoleucine, leucine, valine and tyrosine and the less abundant methionine and tryptophan, have the largest folding free energy changes. This indicates that the recurrent structural motifs, as we define them, describe recurrent structural patterns that are important for protein stability. In view of their properties, such structural motifs are potentially useful for inter-residue contact prediction and protein structure refinement.

Keywords
Amino Acid Motifs, Amino Acid Substitution, Mutation, Missense, Protein Folding, Proteins/chemistry, Proteins/genetics, Sequence Analysis, Protein/methods
Pubmed
Web of science
Open Access
Yes
Create date
05/02/2018 14:58
Last modification date
21/08/2019 6:37
Usage data