期刊
SCIENCE
卷 300, 期 5628, 页码 2061-2065出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1084398
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资金
- NIAMS NIH HHS [AR26846, AR44420] Funding Source: Medline
- NIGMS NIH HHS [R01 GM065367, GM65367] Funding Source: Medline
- PHPPO CDC HHS [PHS 5 T32 GM08276] Funding Source: Medline
Myosin V is a dimeric molecular motor that moves processively on actin, with the center of mass moving similar to37 nanometers for each adenosine triphosphate hydrolyzed. We have labeled myosin V with a single fluorophore at different positions in the light-chain domain and measured the step size with a standard deviation of <1.5 nanometers, with 0.5-second temporal resolution, and observation times of minutes. The step size alternates between 37 + 2x nm and 37 - 2x, where x is the distance along the direction of motion between the dye and the midpoint between the two heads. These results strongly support a hand-over-hand model of motility, not an inchworm model.
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