Correlated mutations and residue contacts in proteins.

@article{citeulike:613990, abstract = {The maintenance of protein function and structure constrains the evolution of amino acid sequences. This fact can be exploited to interpret correlated mutations observed in a sequence family as an indication of probable physical contact in three dimensions. Here we present a simple and general method to analyze correlations in mutational behavior between different positions in a multiple sequence alignment. We then use these correlations to predict contact maps for each of 11 protein families and compare the result with the contacts determined by crystallography. For the most strongly correlated residue pairs predicted to be in contact, the prediction accuracy ranges from 37 to 68\% and the improvement ratio relative to a random prediction from 1.4 to 5.1. Predicted contact maps can be used as input for the calculation of protein tertiary structure, either from sequence information alone or in combination with experimental information.}, address = {Protein Design Group, European Molecular Biology Laboratory, Heidelberg, Germany.}, author = {G\"{o}bel, U. and Sander, C. and Schneider, R. and Valencia, A. }, citeulike-article-id = {613990}, doi = {http://dx.doi.org/10.1002/prot.340180402}, issn = {0887-3585}, journal = {Proteins}, keywords = {contact, correlated-mutation}, month = {April}, number = {4}, pages = {309--317}, posted-at = {2007-11-26 11:48:52}, priority = {2}, title = {Correlated mutations and residue contacts in proteins.}, url = {http://dx.doi.org/10.1002/prot.340180402}, volume = {18}, year = {1994} }

TY - JOUR ID - citeulike:613990 L3 - citeulike-article-id:613990 TI - Correlated mutations and residue contacts in proteins. JF - Proteins VL - 18 IS - 4 SP - 309 EP - 317 AD - Protein Design Group, European Molecular Biology Laboratory, Heidelberg, Germany. SN - 0887-3585 N2 - The maintenance of protein function and structure constrains the evolution of amino acid sequences. This fact can be exploited to interpret correlated mutations observed in a sequence family as an indication of probable physical contact in three dimensions. Here we present a simple and general method to analyze correlations in mutational behavior between different positions in a multiple sequence alignment. We then use these correlations to predict contact maps for each of 11 protein families and compare the result with the contacts determined by crystallography. For the most strongly correlated residue pairs predicted to be in contact, the prediction accuracy ranges from 37 to 68% and the improvement ratio relative to a random prediction from 1.4 to 5.1. Predicted contact maps can be used as input for the calculation of protein tertiary structure, either from sequence information alone or in combination with experimental information. KW - contact KW - correlated-mutation AU - Göbel, U AU - Sander, C AU - Schneider, R AU - Valencia, A PY - 1994/04// UR - http://dx.doi.org/10.1002/prot.340180402 ER -