Electrostatic effects on the α-helix and β-strand formation of BPTI(16-36) studied by Monte Carlo simulated annealing

Journal of Peptide Research

Volumn 54, Issue 3, 1999, Pages 230-236

  Nakazawa, Takashi ^a   Okamoto, Y ^b  

^a NARA WOMEN'S UNIVERSITY   (Japan)

^b GRADUATE UNIVERSITY FOR ADVANCED STUDIES   (Japan)

Author keywords

Bovine pancreatic trypsin inhibitor; Dielectric constant; Electrostatic interaction; Monte Carlo simulated annealing, protein folding; Secondary structure

Indexed keywords

ALPHA HELIX; ARTICLE; ELECTRIC ACTIVITY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; SYSTEM ANALYSIS;

ALGORITHMS; AMINO ACID SEQUENCE; APROTININ; CRYSTALLOGRAPHY, X-RAY; MODELS, MOLECULAR; MODELS, STRUCTURAL; MOLECULAR SEQUENCE DATA; MONTE CARLO METHOD; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; THERMODYNAMICS;

BOVINAE;

EID: 0032829801     PISSN: 1397002X     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3011.1999.00081.x     Document Type: Article

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