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
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.
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