A novel method reveals that solvent water favors polyproline II over β-strand conformation in peptides and unfolded proteins: Conditional hydrophobic accessible surface area (CHASA)

Protein Science

Volumn 14, Issue 1, 2005, Pages 111-118

  Fleming, Patrick J ^a   Fitzkee, Nicholas C ^a   Mezei, Mihaly ^b   Srinivasan, Rajgopal ^c   Rose, George D ^a  

^a JOHNS HOPKINS UNIVERSITY   (United States)

^b NEW YORK UNIVERSITY   (United States)

^c TATA CONSULTANCY SERVICES   (India)

Author keywords

CHASA; Coil library; Conditional hydrophobic accessible surface area; Polyproline II; Probability density map; Solvation energy

Indexed keywords

PROLINE; SOLVENT;

AQUEOUS SOLUTION; ARTICLE; CONDITIONAL HYDROPHOBIC ACCESSIBLE SURFACE AREA; HYDROGEN BOND; HYDROPHOBICITY; NONHUMAN; PEPTIDE ANALYSIS; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; SOLVATION; STRUCTURE ANALYSIS; SURFACE PROPERTY; VALIDATION PROCESS;

HYDROGEN BONDING; HYDROPHOBICITY; OXYGEN; PEPTIDES; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEINS; SURFACE PROPERTIES; WATER;

EID: 11144230087     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.041047005     Document Type: Article

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