Solution NMR studies reveal no global flexibility in the catalytic domain of CDC25B

Proteins: Structure, Function and Bioinformatics

Volumn 82, Issue 11, 2014, Pages 2889-2895

  Lund, George ^a   Cierpicki, Tomasz ^a  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

Author keywords

CDC25B; Model free analysis; NMR dynamics; Protein dynamics; Protein structure; RDC

Indexed keywords

CDC25B PHOSPHATASE; PHOSPHATASE; UNCLASSIFIED DRUG; CDC25B PROTEIN, HUMAN; PROTEIN TYROSINE PHOSPHATASE; SOLUTION AND SOLUBILITY;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CONFORMATION; CROSS COUPLING REACTION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PREDICTION; PRIORITY JOURNAL; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; METABOLISM; PROTEIN CONFORMATION; SOLUTION AND SOLUBILITY;

CATALYTIC DOMAIN; CDC25 PHOSPHATASES; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; PROTEIN CONFORMATION; SOLUTIONS;

EID: 84923351947     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24581     Document Type: Article

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