Please use this identifier to cite or link to this item:
https://lib.hpu.edu.vn/handle/123456789/22254
Full metadata record
DC Field | Value | Language |
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dc.contributor.author | Morgan, Hugh P. | en_US |
dc.contributor.author | Zhong, Wenhe | en_US |
dc.contributor.author | McNae, Iain W. | en_US |
dc.date.accessioned | 2016-07-18T06:49:05Z | |
dc.date.available | 2016-07-18T06:49:05Z | |
dc.date.issued | 2014 | en_US |
dc.identifier.other | HPU4160413 | en_US |
dc.identifier.uri | https://lib.hpu.edu.vn/handle/123456789/22254 | en_US |
dc.description.abstract | The 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.extent | 14 p. | en_US |
dc.format.mimetype | application/pdf | en_US |
dc.language.iso | en | en_US |
dc.subject | Biochemistry | en_US |
dc.subject | Biophysics | en_US |
dc.subject | Structural biology | en_US |
dc.subject | Apoenzyme | en_US |
dc.subject | Leishmania | en_US |
dc.subject | Trypanosoma | en_US |
dc.title | Structures of pyruvate kinases display evolutionarily divergent allosteric strategies | en_US |
dc.type | Article | en_US |
dc.size | 2.13MB | en_US |
dc.department | Education | en_US |
Appears in Collections: | Education |
Files in This Item:
File | Description | Size | Format | |
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0296_Structuresofpyruvatekinases.pdf Restricted Access | 2.19 MB | Adobe PDF | ![]() View/Open Request a copy |
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