Phenylalanine fluorescence studies of calcium binding to N-domain fragments of Paramecium calmodulin mutants show increased calcium affinity correlates with increased disorder

Protein Science

Volumn 10, Issue 9, 2001, Pages 1758-1768

  Vanscyoc, W S ^a   Shea, M A ^a  

^a UNIVERSITY OF IOWA   (United States)

Author keywords

Ca2+; CaM; Cooperativity; Gel permeation chromatography; Hydrodynamics; Sodium channels; Stokes radius; Structure; Thermal stability

Indexed keywords

CALCIUM; CALMODULIN; PHENYLALANINE; SODIUM; SODIUM CHANNEL;

ARTICLE; BINDING AFFINITY; BINDING SITE; CALCIUM BINDING; CONFORMATIONAL TRANSITION; DENATURATION; ENERGY; FLUORESCENCE; GEL PERMEATION CHROMATOGRAPHY; HYDRODYNAMICS; MUTANT; NONHUMAN; PARAMECIUM; PRIORITY JOURNAL; STOICHIOMETRY; THERMOSTABILITY;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CALCIUM; CALMODULIN; FLUORESCENCE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PARAMECIUM; PEPTIDE FRAGMENTS; PHENYLALANINE; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN STRUCTURE, TERTIARY; SPECTROMETRY, FLUORESCENCE; TEMPERATURE; THERMODYNAMICS; WATER;

PARAMECIUM;

EID: 0034854501     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.11601     Document Type: Article

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