dc.creator | Nathaniel, Elizabeth Anne Nalani | |
dc.date.accessioned | 2020-08-21T21:29:28Z | |
dc.date.available | 2010-04-30 | |
dc.date.issued | 2010-04-30 | |
dc.identifier.uri | https://etd.library.vanderbilt.edu/etd-03242010-175917 | |
dc.identifier.uri | http://hdl.handle.net/1803/11198 | |
dc.description.abstract | In this thesis, the structural differences between wild-type band 3 and band 3 Fukuoka, the G130R mutant identified in cases of hereditary spherocytosis associated with reduction of protein 4.2, are examined. The G130R mutation occurs on the solvent-facing side of helix 2 on the globular portion of the cytosolic domain of band 3. Site-directed spin labeling coupled with electron paramagnetic resonance techniques are presented as methods for investigating subtle changes to protein structure. While the overall structure of the band 3 dimer shows little change, side chain mobilities are altered on helix 2. Solvent accessibility, on the other hand, shows that helix 2 maintains its backbone structure and relative orientation on the surface of band 3. I believe these small changes to helix 2 affect the binding of band 3 to ankyrin due to the proximity to their interaction site. | |
dc.format.mimetype | application/pdf | |
dc.subject | erythrocyte cytoskeleton | |
dc.subject | anion exchanger 1 | |
dc.subject | CW-EPR | |
dc.subject | power saturation | |
dc.title | Characterization of Band 3 Variant G130R Using Site-Directed Spin Labeling and Electron Paramagnetic Resonance | |
dc.type | thesis | |
dc.contributor.committeeMember | Al Beth | |
dc.contributor.committeeMember | Hassane Mchaourab | |
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 | 2010-04-30 | |
local.embargo.lift | 2010-04-30 | |
dc.contributor.committeeChair | Charles Cobb | |