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dc.contributor.authorBai, Xiaoyu
Wolynes, Peter G.
dc.date.accessioned 2017-05-09T20:16:06Z
dc.date.available 2017-05-09T20:16:06Z
dc.date.issued 2015
dc.identifier.citation Bai, Xiaoyu and Wolynes, Peter G.. "On the hydrodynamics of swimming enzymes." The Journal of Chemical Physics, 143, no. 16 (2015) AIP Publishing LLC: http://dx.doi.org/10.1063/1.4933424.
dc.identifier.urihttps://hdl.handle.net/1911/94210
dc.description.abstract Several 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.language.iso eng
dc.publisher AIP Publishing LLC
dc.rights Article 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.title On the hydrodynamics of swimming enzymes
dc.type Journal article
dc.citation.journalTitle The Journal of Chemical Physics
dc.contributor.org Center for Theoretical Biological Physics
dc.citation.volumeNumber 143
dc.citation.issueNumber 16
dc.type.dcmi Text
dc.identifier.doihttp://dx.doi.org/10.1063/1.4933424
dc.identifier.pmid 26520553
dc.type.publication publisher version
dc.citation.articleNumber 165101


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