Various strategies of using residual dipolar couplings in NMR-driven protein docking: Application to Lys48-linked di-ubiquitin and validation against 15N-relaxation data

Proteins: Structure, Function and Genetics

Volumn 60, Issue 3, 2005, Pages 367-381

  Van Dijk, Aalt D J ^a   Fushman, David ^b   Bonvin, Alexandre M J J ^a  

^a UTRECHT UNIVERSITY   (Netherlands)

^b Bldg 142   (United States)

Author keywords

Chemical shift perturbation; Di ubiquitin; Diffusion anisotropy; Docking; Protein complexes; Residual dipolar couplings

Indexed keywords

LYSINE; NITROGEN 15; PROTEIN; UBIQUITIN;

ANISOTROPY; ARTICLE; DIFFUSION; DIPOLE; MOLECULAR INTERACTION; NITROGEN NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

ALGORITHMS; COMPUTATIONAL BIOLOGY; CRYSTALLOGRAPHY, X-RAY; LYSINE; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MODELS, STATISTICAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEOMICS; REPRODUCIBILITY OF RESULTS; SOFTWARE; UBIQUITIN; WATER;

EID: 23044484731     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20476     Document Type: Article

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