Heteronuclear NMR studies of E. coli translation initiation factor IF3. Evidence that the inter-domain region is disordered in solution

Journal of Molecular Biology

Volumn 266, Issue 1, 1997, Pages 15-22

  Moreau, Magali ^a   De Cock, Eve ^a   Fortier, Pierre Louis ^c   Garcia, Carlos ^a,d   Albaret, Christine ^a,c   Blanquet, Sylvain ^b   Lallemand, Jean Yves ^a   Dardel, Frédéric ^b  

^a LABORATOIRE DE SYNTHÈSE ORGANIQUE   (France)

^b LABORATOIRE DE BIOCHIMIE   (France)

^c CENTRE D ETUDES DU BOUCHET   (France)

^d SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

Heteronuclear relaxation; Multi domain protein; Protein flexibility; Ribosome; Translation

Indexed keywords

INITIATION FACTOR 3; LYSINE; PROTON;

ARTICLE; CONTROLLED STUDY; ESCHERICHIA COLI; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN STRUCTURE; RIBOSOME; START CODON;

EID: 0031566955     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0756     Document Type: Article

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