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dc.contributor.authorKhataee, Hamidreza
dc.contributor.authorNaseri, Solmaz
dc.contributor.authorZhong, Yongmin
dc.contributor.authorLiew, Alan Wee-Chung
dc.date.accessioned2019-06-19T13:07:35Z
dc.date.available2019-06-19T13:07:35Z
dc.date.issued2018
dc.identifier.issn1868-1743
dc.identifier.doi10.1002/minf.201700092
dc.identifier.urihttp://hdl.handle.net/10072/376378
dc.description.abstractThe ability to predict the cellular dynamics of intracellular transport has enormous potential to impact human health. A key transporter is kinesin‐1, an ATP‐driven molecular motor that shuttles cellular cargos along microtubules (MTs). The dynamics of kinesins depends critically on their unbinding rate from MT, which varies depending on the force direction applied on the motor, i.e. the force‐unbinding rate relation is asymmetric. However, it remains unclear how changing the force direction from resisting (applied against the motion direction) to assisting (applied in the motion direction) alters the kinesin's unbinding and stepping. Here, we propose a theoretical model for the influence of the force direction on the stepping dynamics of a single kinesin. The model shows that the asymmetry of the force‐unbinding rate relation is independent of ATP concentration. It also reveals that the synthesis of ATP from backward stepping under assisting forces is less likely than under resisting forces. It then finds that the unbinding of kinesin in the strongly MT‐bound kinetic states enhances under assisting forces.
dc.description.peerreviewedYes
dc.languageEnglish
dc.publisherWiley - V C H Verlag GmbH & Co. KGaA
dc.publisher.placeGermany
dc.relation.ispartofchapter1700092
dc.relation.ispartofpagefrom1
dc.relation.ispartofpageto7
dc.relation.ispartofissue4
dc.relation.ispartofjournalMolecular Informatics
dc.relation.ispartofvolume37
dc.subject.fieldofresearchTheoretical and Computational Chemistry not elsewhere classified
dc.subject.fieldofresearchMedicinal and Biomolecular Chemistry
dc.subject.fieldofresearchTheoretical and Computational Chemistry
dc.subject.fieldofresearchBiochemistry and Cell Biology
dc.subject.fieldofresearchcode030799
dc.subject.fieldofresearchcode0304
dc.subject.fieldofresearchcode0307
dc.subject.fieldofresearchcode0601
dc.titleUnbinding of Kinesin from Microtubule in the Strongly Bound States Enhances under Assisting Forces
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.facultyGriffith Sciences, School of Information and Communication Technology
gro.hasfulltextNo Full Text
gro.griffith.authorLiew, Alan Wee-Chung
gro.griffith.authorKhataee Gavgani, Hamidreza


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