Abstract
Molecular motors are enzymes that convert chemical potential energy into controlled kinetic energy for mechanical work inside cells. Understanding the biophysics of these motors is essential for appreciating life as well as apprehending diseases that arise from motor malfunction. This review focuses on kinesin motor enzymology with special emphasis on the literature that reports the chemistry, structure and physics of several different kinesin superfamily members.
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Abbreviations
- AlFx :
-
Aluminum fluoride
- AMPPCP:
-
Adenosine 5′-(β,γ-methylene)triphosphate
- AMPPNP:
-
Adenosine 5′-(β,γ-imido)triphosphate
- ATP:
-
Adenosine 5′-triphosphate
- ATPγS:
-
Adenosine 5′-(γ-thio)triphosphate
- BeFx :
-
Beryllium fluoride
- E:
-
Kinesin
- FRET:
-
Förster resonance energy transfer
- mant-ATP:
-
2'-(or-3')-O-(N-Methylanthraniloyl) adenosine 5'-triphosphate
- MDCC-PBP:
-
7-Diethylamino-3-((((2-maleimidyl)ethyl)amino)carbonyl) coumarin)-labeled phosphate binding protein
- MT:
-
Microtubule
- SDS-PAGE:
-
Sodium dodecyl sulfate polyacrylamide gel electrophoresis
- SO4 - :
-
Sulfate
- VO4 - :
-
Vanadate
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Acknowledgments
I would like to thank Joseph Eskew for his help with Appendix A, and Kayla Bell, Benjamin Walker, and Jeff Ewer for helpful discussions. I am grateful for comments on the manuscript provided by Claire Walczak and F. Jon Kull.
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Jarod C Cochran declares that he has no conflict of interest.
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Cochran, J. Kinesin Motor Enzymology: Chemistry, Structure, and Physics of Nanoscale Molecular Machines. Biophys Rev 7, 269–299 (2015). https://doi.org/10.1007/s12551-014-0150-6
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DOI: https://doi.org/10.1007/s12551-014-0150-6