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Angewandte Chemie - International Edition

Volumn 52, Issue 2, 2013, Pages 687-690

Direct prediction of NMR residual dipolar couplings from the primary sequence of unfolded proteins

(4) Huang, Jie Rong a Ozenne, Valéry a Jensen, Malene Ringkjøbing a Blackledge, Martin a

a INSTITUT DE BIOLOGIE STRUCTURALE (France)

Author keywords

conformational sampling; intrinsic disorder; NMR spectroscopy; proteins; residual dipolar couplings

Indexed keywords

CONFORMATIONAL ANALYSIS; DIRECT PREDICTION; DISORDERED PROTEINS; INTRINSIC DISORDER; NEAREST NEIGHBORS; PRIMARY SEQUENCES; RESIDUAL DIPOLAR COUPLINGS; SENSITIVE PROBE; UNFOLDED PROTEINS;

NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

PROTEINS;

PROTEIN;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; METHODOLOGY; NUCLEAR MAGNETIC RESONANCE; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN UNFOLDING;

MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN UNFOLDING; PROTEINS;

EID: 84872000544 PISSN: 14337851 EISSN: 15213773 Source Type: Journal
DOI: 10.1002/anie.201206585 Document Type: Article

Times cited : (18)

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