Prodan fluorescence reflects differences in nucleotide-induced conformational states in the myosin head and allows continuous visualization of the ATPase reactions

Biochemistry

Volumn 37, Issue 20, 1998, Pages 7167-7176

  Hiratsuka, Toshiaki ^a  

^a ASAHIKAWA MEDICAL COLLEGE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

6 PROPIONYL 2 (DIMETHYLAMINO)NAPHTHALENE; FLUORESCENT DYE; UNCLASSIFIED DRUG;

ACTIN MYOSIN INTERACTION; ARTICLE; CONFORMATIONAL TRANSITION; ENZYME ACTIVITY; ENZYME BINDING; ENZYME KINETICS; FLUORESCENCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE; STRUCTURE ACTIVITY RELATION;

2-NAPHTHYLAMINE; ACTINS; ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; ANIMALS; CYTIDINE TRIPHOSPHATE; FLUORESCENT DYES; GUANOSINE TRIPHOSPHATE; HYDROLYSIS; INOSINE TRIPHOSPHATE; KINETICS; MYOSIN SUBFRAGMENTS; PROTEIN BINDING; PROTEIN CONFORMATION; RABBITS; RIBONUCLEOTIDES; SPECTROMETRY, FLUORESCENCE; URIDINE TRIPHOSPHATE;

EID: 0032546535     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi973083d     Document Type: Article

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