Cheung, Margaret S.Misiura, Mikita M.Kolomeisky, Anatoly B.Sutton, Gregory D.2018-02-272018-02-272017-10-12http://hdl.handle.net/10657/2584Motor proteins, like kinesins, dyneins, and myosins, are enzymes that convert chemical energy into motion to transport large cellular components that cannot diffuse by themselves. Both kinesins and dyneins provide scaffolding for a large number of motor protein functions such as cell trafficking, cell division, and muscle contraction. Because of their important roles, the malfunctioning of kinesins is associated with a variety of different diseases. Hereditary Spastic Paraplegia (HSP) is one of the neurodegenerative diseases associated with mutated conventional kinesin genes. Here, we investigate mutation K253N, one of the mutations of kinesin-­‐1 gene associated with HSP. This work aims to uncover the molecular basis for the negative effect of mutation K253N on kinesin’s speed. This project was completed with contributions from Mikita M. Misiura and Anatoly B. Kolomeisky from the Center for Theoretical Biological Physics, Rice University and the Department of Chemistry, Rice University.en-USThe author of this work is the copyright owner. UH Libraries and the Texas Digital Library have their permission to store and provide access to this work. Further transmission, reproduction, or presentation of this work is prohibited except with permission of the author(s).The Effect of Mutated K253N on Kinesin's SpeedPoster