A simple tool to explore the distance distribution of correlated mutations in proteins.

Raul Perez-Jimenez, Raquel Godoy-Ruiz, Antonio Parody-Morreale, Beatriz Ibarra-Molero, Jose M Sanchez-Ruiz

Journal: Biophysical chemistry 2006;119(3):240-6

PMID: 16239060

Abstract

The analysis of correlated mutations in protein sequence alignments is of considerable interest, since it may provide useful energetic and even structural information (ideally, residue contacts). However, a number of recent experimental studies support the existence of long-distance communication in proteins, a fact that may lead to correlation between distant residues. We introduce in this work a simple statistical procedure to describe the relation structure--alignments on the basis of the residue--residue distance dependence of the number of residue couples over given thresholds of a correlation measure (such as a covariance value). This procedure may lead to clear pictures of the distance distribution of correlated mutations and may provide a simple but efficient tool to explore the different structural features that are reflected in the sequence alignments.

Address: Departamento de Quimica Fisica, Facultad de Ciencias, Universidad de Granada, Fuentenueva s/n, 18071-Granada, Spain.

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