| Type of Document |
Master's Thesis |
| Author |
Nathaniel, Elizabeth Anne Nalani
|
| URN |
etd-03242010-175917 |
| Title |
Characterization of Band 3 Variant G130R Using Site-Directed Spin Labeling and Electron Paramagnetic Resonance |
| Degree |
Master of Science |
| Department |
Chemical and Physical Biology |
| Advisory Committee |
| Advisor Name |
Title |
| Charles Cobb |
Committee Chair |
| Al Beth |
Committee Member |
| Hassane Mchaourab |
Committee Member |
|
| Keywords |
- erythrocyte cytoskeleton
- anion exchanger 1
- CW-EPR
- power saturation
|
| Date of Defense |
2010-03-01 |
| Availability |
unrestricted |
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.
|
| Files |
| Filename |
Size |
Approximate Download Time
(Hours:Minutes:Seconds)
|
| 28.8 Modem |
56K Modem |
ISDN (64 Kb) |
ISDN (128 Kb) |
Higher-speed Access |
| |
Nathaniel.pdf |
3.60 Mb |
00:16:40 |
00:08:34 |
00:07:30 |
00:03:45 |
00:00:19 |
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