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DC Field | Value | Language |
---|---|---|
dc.contributor.author | Dutta, Sandipan | - |
dc.date.accessioned | 2024-03-04T04:25:40Z | - |
dc.date.available | 2024-03-04T04:25:40Z | - |
dc.date.issued | 2018 | - |
dc.identifier.uri | https://www.pnas.org/doi/full/10.1073/pnas.1717844115 | - |
dc.identifier.uri | http://dspace.bits-pilani.ac.in:8080/jspui/xmlui/handle/123456789/14490 | - |
dc.description.abstract | There is mounting evidence that enzyme diffusivity is enhanced when the enzyme is catalytically active. Here, using superresolution microscopy [stimulated emission-depletion fluorescence correlation spectroscopy (STED-FCS)], we show that active enzymes migrate spontaneously in the direction of lower substrate concentration (“antichemotaxis”) by a process analogous to the run-and-tumble foraging strategy of swimming microorganisms and our theory quantifies the mechanism. The two enzymes studied, urease and acetylcholinesterase, display two families of transit times through subdiffraction-sized focus spots, a diffusive mode and a ballistic mode, and the latter transit time is close to the inverse rate of catalytic turnover. This biochemical information-processing algorithm may be useful to design synthetic self-propelled swimmers and nanoparticles relevant to active materials. Executed by molecules lacking the decision-making circuitry of microorganisms, antichemotaxis by this run-and-tumble process offers the biological function to homogenize product concentration, which could be significant in situations when the reactant concentration varies from spot to spot. | en_US |
dc.language.iso | en | en_US |
dc.publisher | PNAS | en_US |
dc.subject | Physics | en_US |
dc.subject | Antichemotaxis | en_US |
dc.subject | Enzyme | en_US |
dc.title | Enzyme leaps fuel antichemotaxis | en_US |
dc.type | Article | en_US |
Appears in Collections: | Department of Physics |
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