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Information‐theoretic dissection of pairwise contact potentials
Author(s) -
Cline Melissa S.,
Karplus Kevin,
Lathrop Richard H.,
Smith Temple F.,
Rogers Robert G.,
Haussler David
Publication year - 2002
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.10198
Subject(s) - pairwise comparison , mutual information , representation (politics) , charge (physics) , computer science , sampling (signal processing) , biological system , chemistry , artificial intelligence , theoretical computer science , biology , physics , computer vision , filter (signal processing) , quantum mechanics , politics , political science , law
Pairwise contact potentials have a long, successful history in protein structure prediction. They provide an easily‐estimated representation of many attributes of protein structures, such as the hydrophobic effect. In order to improve on existing potentials, one should develop a clear understanding of precisely what information they convey. Here, using mutual information, we quantified the information in amino acid potentials, and the importance of hydropathy, charge, disulfide bonding, and burial. Sampling error in mutual information was controlled for by estimating how much information cannot be attributed to sampling bias. We found the information in amino acid contacts to be modest: 0.04 bits per contact. Of that, only 0.01 bits of information could not be attributed to hydropathy, charge, disulfide bonding, or burial. Proteins 2002;49:7–14. © 2002 Wiley‐Liss, Inc.