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김철민

Ghim, Cheol-Min
Physical Biology Biological Physics Lab.
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dc.citation.endPage 051910/5 -
dc.citation.number 5 -
dc.citation.startPage 051910/1 -
dc.citation.title PHYSICAL REVIEW E -
dc.citation.volume 66 -
dc.contributor.author Ghim, Cheol-Min -
dc.contributor.author Park, JM -
dc.date.accessioned 2023-12-22T11:36:36Z -
dc.date.available 2023-12-22T11:36:36Z -
dc.date.created 2014-10-10 -
dc.date.issued 2002-11 -
dc.description.abstract We propose a physical model for the gating mechanism of ionic channels. First, we investigate the fluctuation-mediated interactions between two proteins imbedded in a cellular membrane and find that the interaction depends on their orientational configuration as well as the distance between them. The orientational dependence of interactions arises from the fact that the noncircular cross-sectional shapes of individual proteins constrain fluctuations of the membrane differently according to their orientational configuration. Then, we apply these interactions to ionic channels composed of four, five, and six proteins. As the gating stimulus creates the changes in the structural shape of proteins composing ionic channels, the orientational configuration of the ionic channels changes due to the free energy minimization, and ionic channels are open or closed according to the conformation thereof. -
dc.identifier.bibliographicCitation PHYSICAL REVIEW E, v.66, no.5, pp.051910/1 - 051910/5 -
dc.identifier.doi 10.1103/PhysRevE.66.051910 -
dc.identifier.issn 2470-0045 -
dc.identifier.scopusid 2-s2.0-37649030922 -
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/7100 -
dc.identifier.url http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=37649030922 -
dc.identifier.wosid 000179630800074 -
dc.language 영어 -
dc.publisher American Physical Society -
dc.title Physical model for the gating mechanism of ionic channels -
dc.type Article -
dc.description.isOpenAccess FALSE -
dc.description.journalRegisteredClass scopus -

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