NMR characterization of the NADP(H)-binding domain of Escherichia coli transhydrogenase: Sequential assignment and global fold

FEBS Letters

Volumn 458, Issue 2, 1999, Pages 180-184

  Johansson, Carina ^a   Bergkvist, Anders ^a   Fjellström, Ola ^a   Rydström, Jan ^a   Karlsson, B Göran ^b  

^a UNIVERSITY OF GOTHENBURG   (Sweden)

^b CHALMERS UNIVERSITY OF TECHNOLOGY   (Sweden)

Author keywords

Escherichia coli; Global fold; NMR; Transhydrogenase

Indexed keywords

NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) TRANSHYDROGENASE;

ARTICLE; BINDING SITE; ENZYME STRUCTURE; ESCHERICHIA COLI; IN VITRO STUDY; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CARBON ISOTOPES; ESCHERICHIA COLI; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NADP; NADP TRANSHYDROGENASE; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; RHODOSPIRILLUM RUBRUM; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

ESCHERICHIA COLI;

EID: 0032840659     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(99)01156-4     Document Type: Article

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