Physical reasons for the unusual α-helix stabilization afforded by charged or neutral polar residues in alanine-rich peptides

Proceedings of the National Academy of Sciences of the United States of America

Volumn 97, Issue 24, 2000, Pages 13075-13079

  Vila, Jorge A ^a   Ripoll, Daniel R ^b   Scheraga, H A ^b  

^a UNIVERSIDAD NACIONAL DE SAN LUIS   (Argentina)

^b Department of Population Medicine and Diagnostic Sciences   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ALCOHOL; AMINO ACID; CARBON MONOXIDE; GLUTAMINE; LYSINE; OLIGOPEPTIDE; PEPTIDE;

ALPHA HELIX; AMINO ACID SEQUENCE; AQUEOUS SOLUTION; ARTICLE; CONFORMATIONAL TRANSITION; DIELECTRIC CONSTANT; ENERGY; HYDROGEN BOND; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; SIMULATION;

ALANINE; DRUG STABILITY; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MONTE CARLO METHOD; OLIGOPEPTIDES; PEPTIDES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0034700155     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.240455797     Document Type: Article

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