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Information-theoretic dissection of pairwise contact potentials.

Authors
  • Ms, Cline
  • K, Karplus
  • Rh, Lathrop
  • Tf, Smith
  • Jr, Rogers Rg
  • David Haussler
Type
Published Article
Journal
Proteins Structure Function and Bioinformatics
Publisher
Wiley (John Wiley & Sons)
Volume
49
Issue
1
Pages
7–14
Source
UCSC Neuro biomedical-ucsc
License
Unknown

Abstract

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.

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