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dc.contributor.authorTsai, Min-Yehen_US
dc.contributor.authorYuan, Jian-Minen_US
dc.contributor.authorLin, Sheng-Hsienen_US
dc.date.accessioned2015-07-21T08:28:50Z-
dc.date.available2015-07-21T08:28:50Z-
dc.date.issued2015-01-01en_US
dc.identifier.issn0009-4536en_US
dc.identifier.urihttp://dx.doi.org/10.1002/jccs.201400272en_US
dc.identifier.urihttp://hdl.handle.net/11536/124243-
dc.description.abstractIn this work, we present a kinetic analysis for protein aggregation using the kinetic Ising model, which serves as a new application of a previously proposed model [Liang et al., J. Chin. Chem. Soc. 2003, 50, 335]. Considering protein as a single spin unit, we map two states of a unit to the aggregation-prone (AP) and the fibril (F) states. This work shows that the model can successfully capture the nucleation-growth features of protein aggregation from experiments, which offers thermodynamic interpretations of aggregation properties, such as lag-time and fibril stability.en_US
dc.language.isoen_USen_US
dc.subjectProtein aggregationen_US
dc.subjectThermodynamicsen_US
dc.subjectKineticsen_US
dc.subjectIsing modelen_US
dc.titleThermodynamic Insight into Protein Aggregation Using a Kinetic Ising Modelen_US
dc.typeArticleen_US
dc.identifier.doi10.1002/jccs.201400272en_US
dc.identifier.journalJOURNAL OF THE CHINESE CHEMICAL SOCIETYen_US
dc.citation.volume62en_US
dc.citation.spage21en_US
dc.citation.epage25en_US
dc.contributor.department應用化學系zh_TW
dc.contributor.departmentDepartment of Applied Chemistryen_US
dc.identifier.wosnumberWOS:000348005400004en_US
dc.citation.woscount0en_US
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