Evaluation of short-range interactions as secondary structure energies for protein fold and sequence recognition

Proteins: Structure, Function and Genetics

Volumn 36, Issue 3, 1999, Pages 347-356

  Miyazawa, Sanzo ^a,b   Jernigan, Robert L ^b  

^a GUNMA UNIVERSITY   (Japan)

^b NATIONAL CANCER INSTITUTE   (United States)

Author keywords

Empirical potentials; Protein inverse folding; Protein sequence threading; Statistical potentials

Indexed keywords

AMINO ACID SEQUENCE; ARTICLE; ENERGY TRANSFER; EQUILIBRIUM CONSTANT; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; STATISTICAL MODEL; X RAY ANALYSIS;

MATHEMATICS; MODELS, CHEMICAL; OLIGOPEPTIDES; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEINS; THERMODYNAMICS;

EID: 0033566967     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19990815)36:3<347::AID-PROT9>3.0.CO;2-3     Document Type: Article

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