NMR studies of the E140Q mutant of the carboxy-terminal domain of calmodulin reveal global conformational exchange in the Ca2+-saturated state

Biochemistry

Volumn 36, Issue 12, 1997, Pages 3448-3457

  Evenäs, Johan ^a   Thulin, Eva ^a   Malmendal, Anders ^a   Forsén, Sture ^a   Carlström, Göran ^a  

^a LUND UNIVERSITY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; CALMODULIN; GLUTAMIC ACID; HYDROGEN; NITROGEN 15;

ARTICLE; CALCIUM BINDING; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN DOMAIN;

AMINO ACID SEQUENCE; ANIMALS; CALCIUM; CALMODULIN; CATTLE; DROSOPHILA; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS; PROTEIN CONFORMATION;

BOVINAE;

EID: 0030951461     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9628275     Document Type: Article

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