The length of the calmodulin linker determines the extent of transient interdomain association and target affinity

Journal of the American Chemical Society

Volumn 135, Issue 26, 2013, Pages 9648-9651

  Anthis, Nicholas J ^a   Clore, G Marius ^a  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FLEXIBLE LINKERS; INTER-DOMAIN; NMR RELAXATION; PARAMAGNETIC RELAXATION ENHANCEMENTS; RANDOM COIL; TARGET BINDING; TWO DOMAINS; WILD TYPES;

CALCIUM; CAMS; PARAMAGNETISM; PEPTIDES;

CALMODULIN;

CALCIUM ION; CALMODULIN;

ARTICLE; CRYSTAL STRUCTURE; DISSOCIATION CONSTANT; DYNAMICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FUNCTION; SPIN LABELING; WILD TYPE;

CALCIUM; CALMODULIN; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR;

EID: 84879775056     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja4051422     Document Type: Article

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