Mutational analysis of the role of hydrophobic residues in the 338-348 helix on actin in actomyosin interactions

Biochemistry

Volumn 35, Issue 12, 1996, Pages 3670-3676

  Miller, Carl J ^a   Doyle, Tim C ^b   Bobkova, Elena ^a   Botstein, David ^b   Reisler, Emil ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ALPHA ACTIN; MYOSIN ADENOSINE TRIPHOSPHATASE; MYOSIN HEAVY CHAIN;

ACTIN FILAMENT; ACTIN MYOSIN INTERACTION; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; CONFORMATIONAL TRANSITION; GENE MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; SITE DIRECTED MUTAGENESIS;

ACTINS; ACTOMYOSIN; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; BASE SEQUENCE; CIRCULAR DICHROISM; ELECTROPHORESIS, POLYACRYLAMIDE GEL; FLUORESCENCE; KINETICS; MICROFILAMENTS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MYOSIN SUBFRAGMENTS; MYOSINS; PHALLOIDINE; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; TRYPTOPHAN; YEASTS;

EID: 0029972769     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi952645v     Document Type: Article

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