A mutational study of the energy transmission in E. coli ATP synthase
dc.contributor.author | Nguyen, Trang | |
dc.contributor.author | Campos, Dina | |
dc.contributor.author | Ikechukwu, Ifeoma | |
dc.contributor.author | Valdez, Neydy | |
dc.contributor.author | Hernandez-Alvarado, Jose | |
dc.contributor.author | Li, Yunxiang | |
dc.date.accessioned | 2019-04-23T19:21:07Z | |
dc.date.available | 2019-04-23T19:21:07Z | |
dc.date.issued | 2019 | |
dc.description | Creative Arts and Research Symposium | en_US |
dc.description.abstract | ATP 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.sponsorship | Dr. Yunxiang Li | en_US |
dc.identifier.uri | https://hdl.handle.net/11274/11232 | |
dc.language.iso | en_US | en_US |
dc.subject | E. coli | en_US |
dc.subject | Oxidative phosphorylation | en_US |
dc.subject | ATP synthesis/hydrolysis | en_US |
dc.title | A mutational study of the energy transmission in E. coli ATP synthase | en_US |
dc.type | Poster | en_US |
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