Please use this identifier to cite or link to this item: https://lib.hpu.edu.vn/handle/123456789/22254
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dc.contributor.authorMorgan, Hugh P.en_US
dc.contributor.authorZhong, Wenheen_US
dc.contributor.authorMcNae, Iain W.en_US
dc.date.accessioned2016-07-18T06:49:05Z
dc.date.available2016-07-18T06:49:05Z
dc.date.issued2014en_US
dc.identifier.otherHPU4160413en_US
dc.identifier.urihttps://lib.hpu.edu.vn/handle/123456789/22254en_US
dc.description.abstractThe transition between the inactive T-state (apoenzyme) and active R-state (effector bound enzyme) of Trypanosoma cruzi pyruvate kinase (PYK) is accompanied by a symmetrical 8 rigid body rocking motion of the A- and C-domain cores in each of the four subunits, coupled with the formation of additional salt bridges across two of the four subunit interfaces.en_US
dc.format.extent14 p.en_US
dc.format.mimetypeapplication/pdfen_US
dc.language.isoenen_US
dc.subjectBiochemistryen_US
dc.subjectBiophysicsen_US
dc.subjectStructural biologyen_US
dc.subjectApoenzymeen_US
dc.subjectLeishmaniaen_US
dc.subjectTrypanosomaen_US
dc.titleStructures of pyruvate kinases display evolutionarily divergent allosteric strategiesen_US
dc.typeArticleen_US
dc.size2.13MBen_US
dc.departmentEducationen_US
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