Loop I can modulate ADP affinity, ATPase activity, and motility of different scallop myosins. Transient kinetic analysis of S1 isoforms.

@article{KurzawaGoertz1998LoopIC,
  title={Loop I can modulate ADP affinity, ATPase activity, and motility of different scallop myosins. Transient kinetic analysis of S1 isoforms.},
  author={S E Kurzawa-Goertz and Cynthia L. Perreault-Micale and Kathleen M Trybus and Andrew G. Szent-Gy{\"o}rgyi and Michael A. Geeves},
  journal={Biochemistry},
  year={1998},
  volume={37 20},
  pages={7517-25}
}
The striated muscle myosin of Placopecten moves actin faster in in vitro motility assays and has a higher actin-activated ATPase turnover rate than the myosin of the catch muscle. The heavy chain sequences of the two PlacoS1s are almost identical except at the surface loop 1 near the nucleotide binding pocket, where the two sequences vary significantly. Argopecten striated muscle myosin is 96% identical to Placopecten striated myosin, and both move actin with a similar velocity. To identify the… CONTINUE READING

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