Minimum requirements for motility of a processive motor protein.
In: PLoS ONE, Jg. 12 (2017-10-10), Heft 10, S. 1-13
Online
academicJournal
Zugriff:
Motor proteins generally have a two-way coupling between the ATP hydrolysis site, the lever movement and the binding affinity for their track, which allows them to perform efficient stepping. Here we explore the minimal requirements for directed motility based on simpler schemes in which the binding/unbinding from the track is decoupled from the ATPase cycle. We show that a directed power stroke alone is not sufficient for motility, but combined with an asymmetry in force-induced unbinding rates it can generate stepping. The energetic efficiency of such stepping is limited to approximately 20%. We conclude that the allosteric coupling between the ATP hydrolysis and the track binding is not strictly necessary for motility, but it greatly improves its efficiency. [ABSTRACT FROM AUTHOR]
Copyright of PLoS ONE is the property of Public Library of Science and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Titel: |
Minimum requirements for motility of a processive motor protein.
|
---|---|
Autor/in / Beteiligte Person: | Šarlah, Andreja ; Vilfan, Andrej |
Link: | |
Zeitschrift: | PLoS ONE, Jg. 12 (2017-10-10), Heft 10, S. 1-13 |
Veröffentlichung: | 2017 |
Medientyp: | academicJournal |
ISSN: | 1932-6203 (print) |
DOI: | 10.1371/journal.pone.0185948 |
Schlagwort: |
|
Sonstiges: |
|