Long- and short-range interactions in native protein structures are consistent/minimally frustrated in sequence space

Proteins: Structure, Function and Genetics

Volumn 50, Issue 1, 2003, Pages 35-43

  Miyazawa, Sanzo ^a   Jernigan, Robert L ^b  

^a GUNMA UNIVERSITY   (Japan)

^b NONE

Author keywords

Empirical potentials; Inverse protein folding; Protein folding; Protein sequence design; Protein sequence structure compatibility

Indexed keywords

AMINO ACID SEQUENCE; ARTICLE; CORRELATION ANALYSIS; ENERGY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; STATISTICAL ANALYSIS;

AMINO ACID SEQUENCE; AMINO ACIDS; MODELS, STATISTICAL; MOLECULAR STRUCTURE; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEINS;

EID: 0037233452     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10242     Document Type: Article

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