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dc.contributor.authorNguyen, Trang
dc.contributor.authorCampos, Dina
dc.contributor.authorIkechukwu, Ifeoma
dc.contributor.authorValdez, Neydy
dc.contributor.authorHernandez-Alvarado, Jose
dc.contributor.authorLi, Yunxiang
dc.date.accessioned2019-04-23T19:21:07Z
dc.date.available2019-04-23T19:21:07Z
dc.date.issued2019
dc.identifier.urihttps://hdl.handle.net/11274/11232
dc.descriptionCreative Arts and Research Symposiumen_US
dc.description.abstractATP synthase catalyzes ATP synthesis by oxidative phosphorylation. With the unique mechanism and structure of ATP synthase, the energy transmission between the rotor and stator complex plays a vital role to maintain its proper function. Our previous study has discussed that upon γC87K mutation, a stronger interaction with βE381 could refrain the rotor complex from smooth spin, leading to insufficient energy coupling. In this study, we engineered alanine mutations to these residues to mimic a weaker rotor/stator interaction, and we found that multiple alanine mutation also impairs the enzyme performance. This research will add more pieces to understand the energy flow in ATP synthase.en_US
dc.description.sponsorshipDr. Yunxiang Lien_US
dc.language.isoen_USen_US
dc.subjectE. colien_US
dc.subjectOxidative phosphorylationen_US
dc.subjectATP synthesis/hydrolysisen_US
dc.titleA mutational study of the energy transmission in E. coli ATP synthaseen_US
dc.typePosteren_US


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