On the hydrodynamics of swimming enzymes

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. Swim...

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Bibliographic Details
Published inThe Journal of chemical physics Vol. 143; no. 16; p. 165101
Main Authors Bai, Xiaoyu, Wolynes, Peter G.
Format Journal Article
LanguageEnglish
Published United States American Institute of Physics 28.10.2015
Subjects
Allosteric Regulation
Animals
Biocatalysis
Correlation analysis
Diffusion
Enzymes
Experiments
Fluid dynamics
Fluid flow
Fluorescence
High temperature effects
Humans
Hydrodynamics
Kinetics
Models, Biological
Swimming
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ISSN0021-9606
1089-7690
DOI10.1063/1.4933424

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Summary: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.
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ISSN:0021-9606
1089-7690
DOI:10.1063/1.4933424