APPROACHES TO CHARACTERIZE UBIQUITIN CARBOXY-TERMINAL HYDROLASE L1 BY PROTEOLYTIC MAPPING
| dc.contributor.advisor | Fenselau, Catherine | en_US |
| dc.contributor.author | Smith, Natasha Nicole | en_US |
| dc.contributor.department | Chemistry | en_US |
| dc.contributor.publisher | Digital Repository at the University of Maryland | en_US |
| dc.contributor.publisher | University of Maryland (College Park, Md.) | en_US |
| dc.date.accessioned | 2006-02-04T08:08:38Z | |
| dc.date.available | 2006-02-04T08:08:38Z | |
| dc.date.issued | 2005-12-13 | en_US |
| dc.description.abstract | Ubiquitin carboxy-terminal hydrolase-L1 is a member of a class of deubiquitinating enzymes that functions to bind and stabilize ubiquitin, and, thereby, plays a role in the protein degradation of targeted substrates. It is of interest to the research communities in cancer and mental health because of it's suggested roles in neurological disorders and some carcinomas. Here, the recombinant form of this protein is sequenced and characterized using proteomic and mass spectrometry methods. Sixty-nine percent sequence coverage of recombinant UCH-L1 is achieved. | en_US |
| dc.format.extent | 606604 bytes | |
| dc.format.mimetype | application/pdf | |
| dc.identifier.uri | http://hdl.handle.net/1903/3283 | |
| dc.language.iso | en_US | |
| dc.subject.pqcontrolled | Chemistry, Analytical | en_US |
| dc.title | APPROACHES TO CHARACTERIZE UBIQUITIN CARBOXY-TERMINAL HYDROLASE L1 BY PROTEOLYTIC MAPPING | en_US |
| dc.type | Thesis | en_US |
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