Thesis Topic Details
Topic ID: |
868 | |
Title: |
Evolution of transglutaminases from papain-like cysteine proteases | |
Supervisor: |
Merridee Wouters | |
Research Area: |
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| Associated Staff | ||
|---|---|---|
Assessor: |
Marc Wilkins | |
| Topic Details | ||
Status: |
Active | |
Type: |
Research | |
Programs: |
BINF | |
Group Suitable: |
No | |
Industrial: |
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Pre-requisites: |
An interest in proteins and protein structure. Ability to program in perl. Familarity with a Unix-based environment. | |
Description: |
Transglutaminases are eukaryotic enzymes catalysing a variety of post-translational protein modifications including cross-linking of lysine and glutamine residues. Cross-links confer extra structural rigidity as well as resistance to proteolysis and are an essential component of important biological processes such as blood coagulation, hardening of the fertilization envelope and extracellular matrix assembly. Interestingly, these anabolic enzymes are thought to be descended from degradative enzymes, the papain-like cysteine proteases, based on similarities in structure and catalytic residues. In this study, structure/function changes in transglutaminases and related proteins will be investigated using structural comparison and phylogenetic techniques. Offered in conjuction with Dr Siiri Iismaa and Professor Bob Graham. A benchwork component is available if desired. | |
Comments: |
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| Past Student Reports | ||
| No Reports Available. Contact the supervisor for more information.
Check out all available reports in the CSE Thesis Report Library. NOTE: only current CSE students can login to view and select reports to download. |
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