Direct use of 15N relaxation rates as experimental restraints on molecular shape and orientation for docking of protein-protein complexes

Journal of the American Chemical Society

Volumn 132, Issue 17, 2010, Pages 5987-5989

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

^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

ATOMIC COORDINATE; DIFFUSION TENSOR; DIRECT USE; H-BONDS; HIV-1 PROTEASE; MOLECULAR SHAPES; N-TERMINAL DOMAINS; PRIOR INFORMATION; PROTEIN-PROTEIN COMPLEXES; PROTEIN-PROTEIN DOCKING; PSEUDOPOTENTIALS; RELAXATION RATES; ROTATIONAL DIFFUSION; SPECIFIC ORIENTATION; STRUCTURE CALCULATION;

DOCKING; MOLECULAR ORIENTATION; PHOSPHATASES; PROTEINS;

TENSORS;

DIMER; HYDROGEN; NITROGEN 15; NITROGEN; PROTEIN;

ACCURACY; ARTICLE; CALCULATION; CHEMICAL STRUCTURE; CONTROLLED STUDY; HYDROGEN BOND; MOLECULAR SIZE; PROTEIN PROTEIN INTERACTION; PROTON NUCLEAR MAGNETIC RESONANCE; CHEMISTRY; PROTEIN CONFORMATION;

NITROGEN ISOTOPES; PROTEIN CONFORMATION; PROTEINS;

EID: 77951685863     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja101842n     Document Type: Article

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