dc.creator | Matthews, Gage Franklin | |
dc.date.accessioned | 2020-08-22T17:34:22Z | |
dc.date.available | 2012-08-06 | |
dc.date.issued | 2012-08-06 | |
dc.identifier.uri | https://etd.library.vanderbilt.edu/etd-07182012-102603 | |
dc.identifier.uri | http://hdl.handle.net/1803/13175 | |
dc.description.abstract | The structural analysis of the sodium-calcium exchanger NCX1.1 is presented in this thesis. I explore the background information and previous research detailing NCX1.1 and its mechanism. I also explain some of the technical and important details of the primary method used in this research, which is electron paramagnetic resonance (EPR). Using EPR, I found that a small alpha-helix of NCX1.1 undergoes no conformational change upon the binding of calcium ions to the protein. Also, the results suggest that another region, a small unstructured loop, may undergo some change when calcium ions are bound. This opens the door to future research on this protein and the mechanism of its activity. | |
dc.format.mimetype | application/pdf | |
dc.subject | calcium | |
dc.subject | cardiac | |
dc.subject | ion transporters | |
dc.subject | structural biology | |
dc.subject | electron paramagnetic resonance | |
dc.title | Determination of local movements of the FG-loop and α-helix of sodium-calcium exchanger NCX1.1 upon binding of calcium ions using EPR | |
dc.type | thesis | |
dc.contributor.committeeMember | Hassane Mchaourab | |
dc.contributor.committeeMember | Chuck Sanders | |
dc.type.material | text | |
thesis.degree.name | MS | |
thesis.degree.level | thesis | |
thesis.degree.discipline | Chemical and Physical Biology | |
thesis.degree.grantor | Vanderbilt University | |
local.embargo.terms | 2012-08-06 | |
local.embargo.lift | 2012-08-06 | |
dc.contributor.committeeChair | Albert Beth | |