【摘 要】
:
Microtubule (MT) stability is related to the hydrolysis of the guanosine triphosphate nucleotide (NT) bound to β-tubulin.However, the molecular mechanism by wh
【机 构】
:
MaxPlanckInstituteforColloidsandInterfaces,TheoryandBiosystems,Germany
【出 处】
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8th IUPAP International Conference on Biological Physics(第八届
论文部分内容阅读
Microtubule (MT) stability is related to the hydrolysis of the guanosine triphosphate nucleotide (NT) bound to β-tubulin.However, the molecular mechanism by which the NT state influences the stability of the contacts in the MT lattice remains elusive.With large-scale atomistic simulations and a coarse-grained (CG) analysis of the fluctuations, we identify regions of the protein where local changes are induced by the NT state and by the lateral and longitudinal contacts in the aggregates.The CG analysis provides an indication of how the structural changes affect the interaction strength between the proteins.
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