When I began my thesis work, structures of membrane proteins were few and far between. It was clear that the field was poised for a growth period and offered myriad opportunities for pursuing targets involved in important and interesting biology. It was also clear that there was a dire need to develop new methods and protocols to express, purify and crystallize membrane proteins. Described here are my efforts to contribute to this growth period of membrane protein structural biology. This includes establishing cell culture facilities and protocols for the production of milligram quantities of mammalian membrane proteins, the solving of the structure of the Malarial aquaglyceroporin PfAQP and a carefully designed expression screen that has resulted so far in the crystallization of four proteins. The structure of one of theses proteins, CcmG, has been solved.
|Advisor:||Stroud, Robert M., Julius, David|
|Commitee:||Edwards, Robert, Weissman, Jonathon|
|School:||University of California, San Francisco|
|Department:||Chemistry and Chemical Biology|
|School Location:||United States -- California|
|Source:||DAI-B 69/12, Dissertation Abstracts International|
|Keywords:||Aquaglyceroporin, Crystallography, Expression, Membrane proteins, Purification, Reconstitution|
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