Information-theoretic dissection of pairwise contact potentials

Proteins: Structure, Function and Genetics

Volumn 49, Issue 1, 2002, Pages 7-14

  Cline, Melissa S ^a   Karplus, Kevin ^a   Lathrop, Richard H ^b   Smith, Temple F ^c,d   Rogers Jr , Robert G ^c   Haussler, David ^a  

^a Santa Cruz   (United States)

^b Boston University ^*  (United States)

^c Boston University   (United States)

^d Modular Genetics Inc   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID;

ANALYTICAL ERROR; ARTICLE; DISULFIDE BOND; MATHEMATICAL ANALYSIS; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN STRUCTURE; QUANTITATIVE ANALYSIS; SAMPLING; SURFACE CHARGE;

AMINO ACIDS; DISULFIDES; ELECTROSTATICS; HYDROPHOBICITY; MODELS, BIOLOGICAL; MOLECULAR STRUCTURE; PROTEIN CONFORMATION; PROTEINS; SOLVENTS;

EID: 0036780779     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10198     Document Type: Article

References (28)

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8. Structure-derived hydrophobic potential, hydrophobic potential derived from x-ray structures of globular proteins is able to identify native folds
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11. Factors affecting the ability of energy functions to discriminate correct from incorrect folds
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13. Influence of protein structure databases on the predictive power of statistical pair potentials
14. How do potentials derived from structural databases relate to "true" potentials?
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16. Pairwise contact potentials are unsuitable for protein folding
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19. A method to identify protein sequences that fold into a known three-dimensional structure
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