RMSD and fluorimeter data for "Structural transitions in kinesin minus-end directed microtubule motility"
RMSD and fluorimeter data for "Structural transitions in kinesin minus-end directed microtubule motility"
This entry is for our manuscript, "Structural transitions in kinesin minus-end directed microtubule motility" by Satoki Shibata*, Matthew Y. Wang*, Tsuyoshi Imasaki*, Hideki Shigematsu, Yuanyuan Wei, Chacko Jobichen, Hajime Hagio, J. Sivaraman, Sharyn A. Endow & Ryo Nitta. *Equal contribution Corresponding Authors: Tsuyoshi Imasaki*, Sharyn A. Endow, Ryo Nitta The deposited datasets are 1) beta-strand residue all atom RMSD between kinesin-14 NcdY485K ADP and ADP + free Pi nucleotide states and 2) fluorimeter assays of changes in intrinsic NcdY485K fluorescence upon addition of free Pi . The data are presented in Fig. S9E, and Fig. 6BC and S10, respectively. Files are named for the figures in which the data are shown. A computer script for the RMSD analysis is included. Methods for the fluorimeter assays and data analysis are given.
- Duke University United States
- Kobe University Japan
- Duke NUS Graduate Medical School Singapore
Kinesin motor proteins, Force Production, Power Stroke Fluctuations, Mechanochemical Coupling, Motor Spring-like Element, Mechanical States, Crystal Structure, Cryo-Electron Microscopy, Reversed Motility
Kinesin motor proteins, Force Production, Power Stroke Fluctuations, Mechanochemical Coupling, Motor Spring-like Element, Mechanical States, Crystal Structure, Cryo-Electron Microscopy, Reversed Motility
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