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Dynamic regulation on energy landscape evolution of single-molecule protein by conformational fluctuation

dc.citation.epage0en_US
dc.citation.issue2en_US
dc.citation.spage0en_US
dc.citation.volume86en_US
dc.citation.woscount2en_US
dc.contributor.authorLin, Chien Y.en_US
dc.contributor.authorHuang, Jung Y.en_US
dc.contributor.authorLo, Leu-Weien_US
dc.contributor.department光電工程學系zh_TW
dc.contributor.departmentDepartment of Photonicsen_US
dc.date.accessioned2019-04-03T06:36:54Z
dc.date.available2019-04-03T06:36:54Z
dc.date.issued2012-08-31en_US
dc.description.abstractWe formalize a theory to help explore the effect of conformational fluctuation on the energy landscape evolution of single-molecule protein. Using this formalization, we investigate the photon emission from single photoactivated fluorescent protein. A bimodal regulation on the energy landscape evolution was discovered, and its origin was attributed to slow conformational fluctuations of the protein matrix.en_US
dc.identifier.doi10.1103/PhysRevE.86.021925en_US
dc.identifier.issn1539-3755en_US
dc.identifier.journalPHYSICAL REVIEW Een_US
dc.identifier.urihttp://dx.doi.org/10.1103/PhysRevE.86.021925en_US
dc.identifier.urihttps://ir.lib.nycu.edu.tw/handle/11536/16892
dc.identifier.wosnumberWOS:000308212000005en_US
dc.language.isoen_USen_US
dc.titleDynamic regulation on energy landscape evolution of single-molecule protein by conformational fluctuationen_US
dc.typeArticleen_US

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