Overcoming the problems associated with poor spectra quality of the protein kinase Byr2 using residual dipolar couplings

Protein Science

Volumn 10, Issue 6, 2001, Pages 1260-1263

  Gronwald, Wolfram ^a   Brunner, Eike ^a   Huber, Fritz ^a   Wenzler, Michael ^a   Herrmann, Christian ^b   Kalbitzer, Hans Robert ^a  

^a UNIVERSITY OF REGENSBURG   (Germany)

^b MAX PLANCK INSTITUTE OF MOLECULAR PHYSIOLOGY   (Germany)

Author keywords

Byr2; NMR; Residual dipolar couplings; Structure calculation

Indexed keywords

PROTEIN KINASE B;

ARTICLE; CELL INTERACTION; EFFECTOR CELL; ENZYME STRUCTURE; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; SIGNAL TRANSDUCTION; STRUCTURE ANALYSIS;

BIOCHEMISTRY; FUNGAL PROTEINS; MAGNETIC RESONANCE SPECTROSCOPY; MAP KINASE KINASE KINASES; MITOGEN-ACTIVATED PROTEIN KINASES; MODELS, MOLECULAR; PROTEIN CONFORMATION; SCHIZOSACCHAROMYCES; SCHIZOSACCHAROMYCES POMBE PROTEINS;

EID: 0035000531     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.43201     Document Type: Article

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