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dc.contributor.authorLouie, Elizabeth Aprilen_US
dc.date.accessioned2009-10-06T21:47:31Z
dc.date.available2009-10-06T21:47:31Z
dc.date.issued2005en_US
dc.identifier.otherb56437389en_US
dc.identifier.other70662075en_US
dc.identifier.otherThesis 55510en_US
dc.identifier.urihttp://hdl.handle.net/1773/8488
dc.descriptionThesis (Ph. D.)--University of Washington, 2005.en_US
dc.description.abstractSolid-state nuclear magnetic resonance methods were used to characterize the structure of biological molecules in lyophilized and hydrated environments with and without the presence of other molecules such as drugs, lipids, and surfaces. Revealing the structure of biomolecules by mimicking its natural environment, information about their potential function may be realized. Several small model compounds and double-stranded DNAs were synthesized with an unique phosphorous label and either a single fluorine or trifluoromethyl label. The distance between the phosphorous and fluorine(s) where measured using the heteronuclear REDOR experiment to determine enhancement of dipolar coupling due to a trifluoromethyl group as compared to a single fluorine group. Due to increased dephasing of the trifluoromethyl group it is a promising labeling method to determine drug and biological molecule interactions. In using methods to measure distances between atoms, changes in the secondary structure of a dsDNA in the presence of an antibiotic drug can be monitored. The secondary structure of peptides were also determined but with implementing double quantum DRAWS experiments. These homonuclear dipolar recoupling experiments were implemented to determine torsion (φ and psi) angles of a peptide in a lipid bilayer environment as well as peptides adsorbed on a charged surface. The secondary structure of an amphipathic peptide was compared when it was covalently attached to a resin versus adsorbed to a charged surface.en_US
dc.format.extentxiv, 181 p.en_US
dc.language.isoen_USen_US
dc.rightsCopyright is held by the individual authors.en_US
dc.rights.urien_US
dc.subject.otherTheses--Chemistryen_US
dc.titleSolid-State NMR: investigations of biomolecular structureen_US
dc.typeThesisen_US


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