Full metadata record
DC Field | Value | Language |
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dc.citation.endPage | 18 | - |
dc.citation.number | 1 | - |
dc.citation.startPage | 14 | - |
dc.citation.title | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | - |
dc.citation.volume | 115 | - |
dc.contributor.author | Jee, Ah-Young | - |
dc.contributor.author | Dutta, Sandipan | - |
dc.contributor.author | Cho, Yoon-Kyoung | - |
dc.contributor.author | Tlusty, Tsvi | - |
dc.contributor.author | Granick, Steve | - |
dc.date.accessioned | 2023-12-21T21:15:45Z | - |
dc.date.available | 2023-12-21T21:15:45Z | - |
dc.date.created | 2018-01-03 | - |
dc.date.issued | 2018-01 | - |
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. | - |
dc.identifier.bibliographicCitation | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.115, no.1, pp.14 - 18 | - |
dc.identifier.doi | 10.1073/pnas.1717844115 | - |
dc.identifier.issn | 0027-8424 | - |
dc.identifier.scopusid | 2-s2.0-85040163828 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/23143 | - |
dc.identifier.url | http://www.pnas.org/content/115/1/14.abstract | - |
dc.identifier.wosid | 000419128700019 | - |
dc.language | 영어 | - |
dc.publisher | NATL ACAD SCIENCES | - |
dc.title | Enzyme leaps fuel antichemotaxis | - |
dc.type | Article | - |
dc.description.isOpenAccess | TRUE | - |
dc.relation.journalWebOfScienceCategory | Multidisciplinary Sciences | - |
dc.relation.journalResearchArea | Science & Technology - Other Topics | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordAuthor | enzyme | - |
dc.subject.keywordAuthor | chemotaxis | - |
dc.subject.keywordAuthor | active matter | - |
dc.subject.keywordAuthor | FCS | - |
dc.subject.keywordAuthor | fluorescence correlation spectroscopy | - |
dc.subject.keywordPlus | FLUORESCENCE CORRELATION SPECTROSCOPY | - |
dc.subject.keywordPlus | PROTEIN MACHINES | - |
dc.subject.keywordPlus | CHEMOTAXIS | - |
dc.subject.keywordPlus | GENERATION | - |
dc.subject.keywordPlus | DIFFUSION | - |
dc.subject.keywordPlus | MOLECULES | - |
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