This study focused on the structural genomics of granulin/epithelin modules (GEMs). Expression, purification and NMR studies of 14 out of all known 19 zebrafish GEMs allowed an assessment of the degree of structural diversity in their C-terminal subdomains. Very interestingly, one well-folded zebrafish GEM was obtained, and its three-dimensional structure was determined with high accuracy using NOE, H-bond, dihedral angle and residue dipolar coupling constraints. Solution structure determination and 15N NMR relaxation measurements indicate that one unique proline residue of the zebrafish GEM may confer the well-structured and stable folding property of the stack of all four beta-hairpins in contrast to other members of the GEM protein family.
| Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.81452 |
| Date | January 2004 |
| Creators | Wang, Ping, 1968 Feb. 17- |
| Publisher | McGill University |
| Source Sets | Library and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada |
| Language | English |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
| Format | application/pdf |
| Coverage | Master of Science (Department of Biochemistry.) |
| Rights | All items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated. |
| Relation | alephsysno: 002166508, proquestno: AAIMR06468, Theses scanned by UMI/ProQuest. |
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