title: A structural perspective on the dynamics of kinesin motors.
abstract: Despite significant fluctuation under thermal noise, biological machines in cells perform their tasks with exquisite precision. Using molecular simulation of a coarse-grained model and theoretical arguments, we envisaged how kinesin, a prototype of biological machines, generates force and regulates its dynamics to sustain persistent motor action. A structure-based model, which can be versatile in adapting its structure to external stresses while maintaining its native fold, was employed to account for several features of kinesin dynamics along the biochemical cycle. This analysis complements our current understandings of kinesin dynamics and connections to experiments. We propose a thermodynamic cycle for kinesin that emphasizes the mechanical and regulatory role of the neck linker and clarify issues related to the motor directionality, and the difference between the external stalling force and the internal tension responsible for the head-head coordination. The comparison between the thermodynamic cycle of kinesin and macroscopic heat engines highlights the importance of structural change as the source of work production in biomolecular machines.
authors.affiliation: School of Computational Sciences, Korea Institute for Advanced Study, Seoul, Republic of Korea. hyeoncb@kias.re.kr
authors.forename: Changbong
authors.initials: C
authors.lastname: Hyeon
authors.forename: José N
authors.initials: JN
authors.lastname: Onuchic
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D001696:Biomechanical Phenomena; D016547:Kinesins / Q000737:chemistry* / Q000378:metabolism; D008870:Microtubules / Q000378:metabolism; D008958:Models, Molecular; D018583:Pliability; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D013816:Thermodynamics
chemical_list: D000255:Adenosine Triphosphate; D016547:Kinesins