Basic interdomain boundary residues in calmodulin decrease calcium affinity of sites I and II by stabilizing helix-helix interactions

Proteins: Structure, Function and Genetics

Volumn 50, Issue 3, 2003, Pages 381-391

  Faga, Laurel A ^a   Sorensen, Brenda R ^a   VanScyoc, Wendy S ^a   Shea, Madeline A ^a  

^a UNIVERSITY OF IOWA   (United States)

Author keywords

Allosteric interactions; Calcium affinity; Calcium binding; Domain organization; Interdomain communication; Protein stability; Tertiary constraints; Thermodynamics

Indexed keywords

AMINO ACID; CALCIUM BINDING PROTEIN; CALMODULIN;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CALCIUM BINDING; CARBOXY TERMINAL SEQUENCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEOTIDE SEQUENCE; PARAMECIUM; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; SIGNAL TRANSDUCTION; THERMODYNAMICS; THERMOSTABILITY;

AMINO ACID SEQUENCE; AMINO ACIDS; ANIMALS; CALCIUM; CALMODULIN; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PARAMECIUM; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; THERMODYNAMICS;

PARAMECIUM;

EID: 0037441514     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10281     Document Type: Article

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