Residual dipolar couplings have been introduced recently as a new type of experimental constraints in biomolecular structure determination by nuclear magnetic resonance (NMR). These interactions are obtained by imparting weak orientational ordering to a biomolecule in a dilute liquid crystal. This results in a partial cancellation of anisotropic interactions such as the chemical shift anisotropy (CSA), the quadrupolar coupling and the dipolar coupling. Because the alignment is weak, only strong interactions manifest. These measurements can be used to refine structure or to define folds in structural genomics projects. Here, I demonstrate the use of a new alignment medium that consists of a nematic Pf1 bacteriophage suspension embedded in an aqueous polyacrylamide gel matrix. In the absence of the gel, the phage particles align spontaneously in the NMR field.
| Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.79148 |
| Date | January 2002 |
| Creators | Trempe, Jean-François |
| Contributors | Gehring, Kalle (advisor) |
| 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: 001974444, proquestno: AAIMQ88318, Theses scanned by UMI/ProQuest. |
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