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Bio
Motor proteins and GTP-binding proteins (G-proteins) share many structural and functional attributes. Molecular motors myosin, dynein and kinesin are prototype biological energy transducers that can be understood at a particularly fine level of detail. The obvious functional output (force and motion) allow the reaction sequence to be probed by single molecule biophysical, chemical and structural studies. A cyclic interaction between actin and myosin transforms free energy of splitting ATP into motion and mechanical work. Modified forms of this mechanism power other cell biological motions such as targeted vesicle transport and cell division. We are using novel biophysical techniques, including nanometer tracking of single fluorescent molecules, bifunctional fluorescent probes and infrared optical traps (laser tweezers) to map the real-time domain motions of the motor proteins.
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Papers共 265 篇Author StatisticsCo-AuthorSimilar Experts
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Xiang Ye,Sravya Kotaru, Shannen Cravens,Shweta Him,Yale E. Goldman, Peng-Hsun Chen,Wenshe Liu,S. Walter Englander,A. Joshua Wand
PROTEIN SCIENCE (2023)
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bioRxiv the preprint server for biology (2023)
Biophysical journalno. 3S1 (2023): 437a-437a
Michael C Owens, Hui Shen,Amber Yanas, Maria Saraí Mendoza-Figueroa,Ellen Lavorando, Xiaoyu Wei,Him Shweta,Hsin-Yao Tang,Yale E Goldman,Kathy Fange Liu
bioRxiv : the preprint server for biology (2023)
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#Papers: 265
#Citation: 14817
H-Index: 60
G-Index: 119
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Activity: 26
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