Please use this identifier to cite or link to this item: https://doi.org/10.1038/s42004-019-0131-6
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dc.titleUnderstanding the catch-bond kinetics of biomolecules on a one-dimensional energy landscape
dc.contributor.authorGuo, S.
dc.contributor.authorEfremov, A.K.
dc.contributor.authorYan, J.
dc.date.accessioned2021-12-29T04:03:58Z
dc.date.available2021-12-29T04:03:58Z
dc.date.issued2019
dc.identifier.citationGuo, S., Efremov, A.K., Yan, J. (2019). Understanding the catch-bond kinetics of biomolecules on a one-dimensional energy landscape. Communications Chemistry 2 (1) : 30. ScholarBank@NUS Repository. https://doi.org/10.1038/s42004-019-0131-6
dc.identifier.issn23993669
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/212219
dc.description.abstractIn spite of extensive investigations, the force-dependent unfolding/rupturing rate k(F) of biomolecules still remains poorly understood. A famous example is the frequently observed switch from catch-bond behaviour, where force anti-intuitively decreases k(F), to slip-bond behaviour where increasing force accelerates k(F). A common consensus in the field is that the catch-to-slip switch behaviour cannot be explained in a one-dimensional energy landscape, while this view is mainly built upon assuming that force monotonically affects k(F) along each available transition pathway. In this work, by applying Kramers kinetic rate theory to a model system where the transition starts from a single native state through a pathway involving sequential peeling of a polymer strand until reaching the transition state, we show the catch-to-slip switch behaviour can be understood in a one-dimensional energy landscape by considering the structural-elastic properties of molecules during transition. Thus, this work deepens our understanding of the force-dependent unfolding/rupturing kinetics of molecules/molecular complexes. © 2019, The Author(s).
dc.publisherSpringer Nature
dc.rightsAttribution 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.sourceScopus OA2019
dc.typeArticle
dc.contributor.departmentMECHANOBIOLOGY INSTITUTE
dc.description.doi10.1038/s42004-019-0131-6
dc.description.sourcetitleCommunications Chemistry
dc.description.volume2
dc.description.issue1
dc.description.page30
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