Thermodynamic propensities of amino acids in the native state ensemble: Implications for fold recognition

Protein Science

Volumn 10, Issue 5, 2001, Pages 1032-1045

  Wrabl, J O ^a   Larson, S A ^a   Hilser, V J ^a  

^a University of Texas Medical Branch School of Medicine   (United States)

Author keywords

Native state ensemble; Protein stability; Protein structure prediction; Residue thermodynamics; Threading and fold recognition

Indexed keywords

AMINO ACID ANALYSIS; AMINO ACID SEQUENCE; ARTICLE; DATA BASE; MOLECULAR RECOGNITION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; SEQUENCE ANALYSIS; THERMODYNAMICS;

ALGORITHMS; AMINO ACIDS; COMPUTATIONAL BIOLOGY; COMPUTER SIMULATION; DATABASES; HYDROGEN; MODELS, MOLECULAR; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEINS; REPRODUCIBILITY OF RESULTS; SEQUENCE ALIGNMENT; SOFTWARE; THERMODYNAMICS;

EID: 0035061715     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.01601     Document Type: Article

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