A novel view of domain flexibility in E. coli adenylate kinase based on structural mode-coupling 15N NMR relaxation

Journal of Molecular Biology

Volumn 315, Issue 2, 2002, Pages 155-170

  Tugarinov, Vitali ^a   Shapiro, Yury E ^a   Liang, Zhichun ^b   Freed, Jack H ^b   Meirovitch, Eva ^a  

^a BAR ILAN UNIVERSITY   (Israel)

^b Department of Population Medicine and Diagnostic Sciences   (United States)

Author keywords

15N spin relaxation; Adenylate kinase; Backbone dynamics; Intrinsic domain flexibility and domain motion; SRLS

Indexed keywords

ADENYLATE KINASE;

ARTICLE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; DIFFUSION; DYNAMICS; ENZYME STRUCTURE; ESCHERICHIA COLI; HYDROGEN BOND; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; STRUCTURE ANALYSIS;

ESCHERICHIA COLI;

EID: 0036290378     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.5231     Document Type: Article

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