Methods of NMR structure refinement: Molecular dynamics simulations improve the agreement with measured NMR data of a C-terminal peptide of GCN4-p1

Journal of Biomolecular NMR

Volumn 47, Issue 3, 2010, Pages 221-235

  Dolenc, Jožica ^a,b   Missimer, John H ^c   Steinmetz, Michel O ^c   Van Gunsteren, Wilfred F ^a  

^a ETH ZURICH   (Switzerland)

^b UNIVERSITY OF LJUBLJANA   (Slovenia)

^c PAUL SCHERRER INSTITUTE   (Switzerland)

Author keywords

3J coupling constants; Local elevation; NMR structure determination; NOE upper bounds; Time averaging

Indexed keywords

PEPTIDE; PEPTIDE GCN4 P16 31; UNCLASSIFIED DRUG;

ARTICLE; CARBOXY TERMINAL SEQUENCE; HYDROGEN BOND; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN CONFORMATION; SIMULATION; TERMINAL SEQUENCE;

BASIC-LEUCINE ZIPPER TRANSCRIPTION FACTORS; MOLECULAR DYNAMICS SIMULATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDES; PROTONS; REPRODUCIBILITY OF RESULTS; SACCHAROMYCES CEREVISIAE PROTEINS; THERMODYNAMICS;

EID: 77954757239     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-010-9425-9     Document Type: Article

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