DIMACS TR: 2002-18

The set of pair-wise correlated sequence positions contributes to determination of the immunoglobulin fold

Authors: Boris Galitsky, Andrey Dementiev and Sergey Shelepin


In this study, we are resolving the contradiction that rather limited number of residues or classes of amino acids (about 10) determines the fold (Immunoglobulin-like) for the sequence of about 100 residues long. Immunoglobulin fold comprises the protein super-families with rather distinguishing sequences with less than 10% identity; their sequence alignment can be accomplished only taking into account the 3D structure. Therefore, we believe that discovering the additional common features of the sequences is necessary to explain the existence of common fold for these (SCOP) superfamilies. The analysis of pair-wise interconnection between residues of the multiple sequence alignment helped us to reveal the set of mutually correlated positions, inherent to almost every super-family of protein fold. Hence, the set of constant positions plus the set of variable but mutually correlated ones can serve as a basis of having the common 3D structure for rather distinguishing protein sequences.

Paper Available at: ftp://dimacs.rutgers.edu/pub/dimacs/TechnicalReports/TechReports/2002/2002-18.ps.gz
DIMACS Home Page