title: A simple tool to explore the distance distribution of correlated mutations in proteins.
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.
authors.affiliation: Departamento de Quimica Fisica, Facultad de Ciencias, Universidad de Granada, Fuentenueva s/n, 18071-Granada, Spain.
authors.forename: Raul
authors.initials: R
authors.lastname: Perez-Jimenez
authors.forename: Raquel
authors.initials: R
authors.lastname: Godoy-Ruiz
authors.forename: Antonio
authors.initials: A
authors.lastname: Parody-Morreale
authors.forename: Beatriz
authors.initials: B
authors.lastname: Ibarra-Molero
authors.forename: Jose M
authors.initials: JM
authors.lastname: Sanchez-Ruiz
mesh_terms: D000596:Amino Acids / Q000032:analysis*; D030562:Databases, Protein; D004926:Escherichia coli / Q000737:chemistry; D008432:Mathematical Computing; D009154:Mutation; D011506:Proteins / Q000737:chemistry* / Q000235:genetics; D016415:Sequence Alignment; D013879:Thioredoxins / Q000737:chemistry* / Q000235:genetics
chemical_list: D000596:Amino Acids; D011506:Proteins; D013879:Thioredoxins