Impact of 15N R 2/ R 1 relaxation restraints on molecular size, shape, and bond vector orientation for NMR protein structure determination with sparse distance restraints

Journal of the American Chemical Society

Volumn 133, Issue 16, 2011, Pages 6154-6157

  Ryabov, Yaroslav ^a   Schwieters, Charles D ^a   Clore, G Marius ^b  

^a NATIONAL INSTITUTES OF HEALTH   (United States)

^b NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BOND VECTOR ORIENTATION; COMPLEX SYSTEMS; DIFFUSION TENSOR; METHYL GROUP; MOLECULAR COORDINATES; MOLECULAR SHAPES; MOLECULAR SIZE; N-TERMINAL DOMAINS; NMR STRUCTURES; NUCLEAR OVERHAUSER ENHANCEMENT; PROTEIN STRUCTURES; UBIQUITIN;

FUNCTIONAL GROUPS; MOLECULAR ORIENTATION; NUCLEAR MAGNETIC RESONANCE; PROTEINS;

TENSORS;

ENZYME; G PROTEIN BETA 3; GUANINE NUCLEOTIDE BINDING PROTEIN; HYDROGEN; N TERMINAL DOMAIN OF ENZYME I; NITROGEN 15; PROTEIN; UBIQUITIN; UNCLASSIFIED DRUG; NITROGEN;

AMINO TERMINAL SEQUENCE; ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; HYDROGEN BOND; MOLECULAR SIZE; NITROGEN NUCLEAR MAGNETIC RESONANCE; NUCLEAR OVERHAUSER EFFECT; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN STRUCTURE; X RAY CRYSTALLOGRAPHY; CHEMICAL STRUCTURE; CHEMISTRY; METHODOLOGY; NUCLEAR MAGNETIC RESONANCE;

MODELS, MOLECULAR; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEINS;

EID: 79954985911     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja201020c     Document Type: Article

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