On the hydrodynamics of swimming enzymes

dc.citation.articleNumber165101
dc.citation.issueNumber16
dc.citation.journalTitleThe Journal of Chemical Physics
dc.citation.volumeNumber143
dc.contributor.authorBai, Xiaoyu
dc.contributor.authorWolynes, Peter G.
dc.contributor.orgCenter for Theoretical Biological Physics
dc.date.accessioned2017-05-09T20:16:06Z
dc.date.available2017-05-09T20:16:06Z
dc.date.issued2015
dc.description.abstractSeveral recent experiments suggest that rather generally the diffusion of enzymes may be augmented through their activity. We demonstrate that such swimming motility can emerge from the interplay between the enzyme energy landscape and the hydrodynamic coupling of the enzyme to its environment. Swimming thus occurs during the transit time of a transient allosteric change. We estimate the velocity during the transition. The analysis of such a swimming motion suggests the final stroke size is limited by the hydrodynamic size of the enzyme. This limit is quite a bit smaller than the values that can be inferred from the recent experiments. We also show that one proposed explanation of the experiments based on reaction heat effects can be ruled out using an extended hydrodynamic analysis. These results lead us to propose an alternate explanation of the fluorescence correlation measurements.
dc.identifier.citationBai, Xiaoyu and Wolynes, Peter G.. "On the hydrodynamics of swimming enzymes." <i>The Journal of Chemical Physics,</i> 143, no. 16 (2015) AIP Publishing LLC: http://dx.doi.org/10.1063/1.4933424.
dc.identifier.doihttp://dx.doi.org/10.1063/1.4933424
dc.identifier.urihttps://hdl.handle.net/1911/94210
dc.language.isoeng
dc.publisherAIP Publishing LLC
dc.rightsArticle is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.
dc.titleOn the hydrodynamics of swimming enzymes
dc.typeJournal article
dc.type.dcmiText
dc.type.publicationpublisher version
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