Influence of Protein Environment on Tryptophan Fluorescence

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Influence of Protein Environment on Tryptophan Fluorescence

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dc.contributor.advisor McMillan, Andrew W en_US
dc.contributor.author McMillan, Andrew William en_US
dc.date.accessioned 2012-09-13T17:28:17Z
dc.date.available 2012-09-13T17:28:17Z
dc.date.issued 2012-09-13
dc.date.submitted 2012 en_US
dc.identifier.other McMillan_washington_0250E_10419.pdf en_US
dc.identifier.uri http://hdl.handle.net/1773/20661
dc.description Thesis (Ph.D.)--University of Washington, 2012 en_US
dc.description.abstract Tryptophan fluorescence is often used as a probe of protein structure. One example of this involved the study how a mutation in catechol O-methyltrasferase produces a less stable protein. Other examples of the use of tryptophan and what factors influence variations in emission energy and quantum yield are discussed. Further investigation of these factors was carried out using two simple peptide systems, followed by mixed molecular dynamics/quantum mechanics simulations to calculate the energetics of quenching by electron transfer. These simulations used a simple quantum model that allowed tight coupling between classical and quantum calculations. It also incorporates potentials from induced dipoles. These simulations resulted in a correlation of quantum yield and charge-transfer energies. Interactions between the charge acceptor and protein stabilized charge in one system, while the other was stabilized by interactions between water and both the charge donor and acceptor. en_US
dc.format.mimetype application/pdf en_US
dc.language.iso en_US en_US
dc.subject electron transfer; fluorescence; methyltransferase; molecular dynamics; quantum mechanics; tryptophan en_US
dc.subject.other Biophysics en_US
dc.subject.other Biochemistry en_US
dc.subject.other Biological chemistry en_US
dc.title Influence of Protein Environment on Tryptophan Fluorescence en_US
dc.type Thesis en_US
dc.embargo.terms No embargo en_US


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