Native atomic burials, supplemented by physically motivated hydrogen bond constraints, contain sufficient information to determine the tertiary structure of small globular proteins

Proteins: Structure, Function and Genetics

Volumn 70, Issue 3, 2008, Pages 971-983

  Pereira De Araújo, Antônio F ^a   Gomes, Antonio L C ^a   Bursztyn, Alexandre A ^a   Shakhnovich, Eugene I ^b  

^a UNIVERSITY OF BRASILIA   (Brazil)

^b HARVARD UNIVERSITY   (United States)

Author keywords

Atomic burial; Computer simulation; Hydrophobic potential; Protein folding; Structure prediction

Indexed keywords

GLOBULAR PROTEIN;

ARTICLE; COMPUTER SIMULATION; ENERGY TRANSFER; HYDROGEN BOND; MOLECULAR DYNAMICS; MONTE CARLO METHOD; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN TERTIARY STRUCTURE;

ALGORITHMS; HYDROGEN BONDING; MODELS, MOLECULAR; MONTE CARLO METHOD; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; PROTEINS; THERMODYNAMICS;

EID: 38549162210     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21571     Document Type: Article

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