β-Hairpins with native-like and non-native hydrogen bonding patterns could form during the refolding of staphylococcal nuclease

Journal of Molecular Graphics and Modelling

Volumn 25, Issue 1, 2006, Pages 103-115

  Patel, Sunita ^a   Sista, Prakash ^a   Balaji, Petety V ^a   Sasidhar, Yellamraju U ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY BOMBAY   (India)

Author keywords

Atom depth; GROMACS; GROMOS96; Hydrogen bonds; Hydrogen deuterium exchange; Peptide; Protein folding

Indexed keywords

ATOM DEPTH; GROMACS; GROMOS96; HYDROGEN-DEUTERIUM EXCHANGE; PEPTIDES; PROTEIN FOLDING;

AMINO ACIDS; CONFORMATIONS; DEUTERIUM; ENZYME KINETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

HYDROGEN BONDS;

ASPARTYLTHREONYLVALYLLYSYLLEUCYLMETHIONYLTYROSYLLYSYLGLYCYLGLUTAMINYL PROLYLMETHIONYLTHREONYLPHENYLALANYLARGININE; BACTERIAL ENZYME; NUCLEASE; PEPTIDE; UNCLASSIFIED DRUG;

ARTICLE; DEUTERIUM HYDROGEN EXCHANGE; HYDROGEN BOND; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTECTION; PROTEIN CONFORMATION; PROTEIN FOLDING; SIMULATION;

AMINO ACID SEQUENCE; COMPUTER SIMULATION; DEUTERIUM EXCHANGE MEASUREMENT; HYDROGEN BONDING; MICROCOCCAL NUCLEASE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY;

EID: 33747873410     PISSN: 10933263     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmgm.2005.11.007     Document Type: Article

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