Orienting domains in proteins using dipolar couplings measured by liquid-state NMR: Differences in solution and crystal forms of maltodextrin binding protein loaded with β-cyclodextrin

Journal of Molecular Biology

Volumn 295, Issue 5, 2000, Pages 1265-1273

  Skrynnikov, Nikolai R ^a   Goto, Natalie K ^a   Yang, Daiwen ^a   Choy, Wing Yiu ^a   Tolman, Joel R ^a   Mueller, Geoffrey A ^a   Kay, Lewis E ^a  

^a UNIVERSITY OF TORONTO   (Canada)

Author keywords

Dipolar couplings; Domain orientation; Maltodextrin binding protein; Protein structure and dynamics; Triple resonance multidimensional NMR

Indexed keywords

BINDING PROTEIN; MALTODEXTRIN;

ARTICLE; CONFORMATIONAL TRANSITION; COVALENT BOND; CRYSTAL STRUCTURE; LIGAND BINDING; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; ORIENTATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN MODIFICATION; PROTEIN PHOSPHORYLATION; PROTEIN STRUCTURE; X RAY CRYSTALLOGRAPHY;

EID: 0034602921     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3430     Document Type: Article

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