A shorter peptide model from staphylococcal nuclease for the folding-unfolding equilibrium of a β-hairpin shows that unfolded state has significant contribution from compact conformational states

Journal of Structural Biology

Volumn 164, Issue 1, 2008, Pages 60-74

  Patel, Sunita ^a   Sasidhar, Yellamraju U ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY BOMBAY   (India)

Author keywords

Free energy landscape; GROMOS96; Hairpin; Kinetics; Molecular dynamics; Protein folding; Staphylococcal nuclease; Unfolded state

Indexed keywords

BACTERIAL ENZYME; NUCLEASE; STAPHYLOCOCCAL NUCLEASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BETA CHAIN; CONFORMATIONAL TRANSITION; HYDROPHOBICITY; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; SIMULATION; STRUCTURE ANALYSIS; THEORETICAL MODEL;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; COMPUTER SIMULATION; HYDROPHOBICITY; MICROCOCCAL NUCLEASE; MODELS, MOLECULAR; PEPTIDE FRAGMENTS; PHASE TRANSITION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY;

EID: 51549100980     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2008.06.003     Document Type: Article

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