Starting-structure dependence of nanosecond timescale intersubstate transitions and reproducibility of MD-derived order parameters

Proteins: Structure, Function and Bioinformatics

Volumn 81, Issue 3, 2013, Pages 499-509

  Zeiske, Tim ^a   Stafford, Kate A ^a   Friesner, Richard A ^a   Palmer, Arthur G ^a  

^a Och Spine at New York Presbyterian Hospitals   (United States)

Author keywords

Autocorrelation function; B3 domain of protein G; Force field; Generalized order parameter; Hydrogen bond; Molecular dynamics simulation; NMR spin relaxation; Protein dynamics; Starting structure

Indexed keywords

BUFFER; HYDROXYL GROUP; IMMUNOGLOBULIN BINDING FACTOR; SODIUM CHLORIDE;

ALGORITHM; ARTICLE; DIFFUSION; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTON TRANSPORT; SIMULATION; STREPTOCOCCUS;

BACTERIAL PROTEINS; COMPUTATIONAL BIOLOGY; GLYCINE; HYDROGEN BONDING; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR DYNAMICS SIMULATION; MUTATION; PROTEIN STRUCTURE, SECONDARY; REPRODUCIBILITY OF RESULTS; STREPTOCOCCUS; TIME FACTORS; WATER;

EID: 84873095042     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24209     Document Type: Article

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