Recurrent Structural Motifs in Non-Homologous Protein Structures

International Journal of Molecular Sciences

Maria U. Johansson¹  Vincent Zoete² 

[1] Vital-IT Group, SIB Swiss Institute of Bioinformatics, CH-1015 Lausanne, Switzerland;Molecular Modelling Group, SIB Swiss Institute of Bioinformatics, CH-1015 Lausanne, Switzerland; E-Mail:

关键词: Delaunay triangulation;    protein fragments;    long-range contacts;    protein folding;    protein structure;    structural motifs;    structure comparison/similarity;    structure prediction;   

DOI  :  10.3390/ijms14047795

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2013 by the authors; licensee MDPI, Basel, Switzerland