Quantifying two-bond 1HN-13CO and one-bond 1Hα-13Cα dipolar couplings of invisible protein states by spin-state selective relaxation dispersion NMR spectroscopy

Journal of the American Chemical Society

Volumn 130, Issue 26, 2008, Pages 8397-8405

  Hansen, D Flemming ^a   Vallurupalli, Pramodh ^a   Kay, Lewis E ^a  

^a UNIVERSITY OF TORONTO   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

EXCITED STATES; MOLECULAR BIOLOGY; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

CHEMICAL-; DYNAMIC PROCESSES; NMR SPECTROS COPY; RELAXATION DISPERSION; RESIDUAL DIPOLAR COUPLINGS; STRUCTURAL INFORMATIONS;

EXPERIMENTS;

AMPHOLYTE; CARBON 13; HYDROGEN; NITROGEN; OXYGEN; CARBON; LIGAND; PROTEIN;

ACCURACY; ARTICLE; CHEMICAL BOND; CHEMICAL REACTION; CONFORMATION; DISPERSION; DYNAMICS; LIGAND BINDING; MAGNETIC FIELD; MEASUREMENT; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTON NUCLEAR MAGNETIC RESONANCE; QUANTITATIVE ANALYSIS; QUANTUM MECHANICS; REACTION ANALYSIS; CHEMISTRY; METHODOLOGY; PROTEIN BINDING; PROTEIN CONFORMATION;

CARBON ISOTOPES; LIGANDS; MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEINS;

EID: 46049083589     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja801005n     Document Type: Article

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