Phenotypically selected mutations in myosin's actin binding domain demonstrate intermolecular contacts important for motor function

Biochemistry

Volumn 36, Issue 28, 1997, Pages 8465-8473

  Giese, Kim C ^a   Spudich, James A ^a,b  

^a STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b STANFORD UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; MUTANT PROTEIN; MYOSIN;

ACTIN MYOSIN INTERACTION; ARTICLE; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN PROTEIN INTERACTION; SARCODINA;

ACTINS; ADENOSINE TRIPHOSPHATE; ANIMALS; BINDING SITES; CLONING, MOLECULAR; DICTYOSTELIUM; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME ACTIVATION; GENE EXPRESSION; KINETICS; MODELS, MOLECULAR; MUTAGENESIS; MYOSIN SUBFRAGMENTS; MYOSINS; PHENOTYPE; PROTEIN CONFORMATION; SPECTROMETRY, FLUORESCENCE;

DICTYOSTELIUM; SARCODINA;

EID: 0030837460     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi963141f     Document Type: Article

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