Solution and Surface Characterization of DNA and Proteins

dc.contributor.advisorStefan Franzen, Committee Chairen_US
dc.contributor.advisorEdmond Bowden, Committee Memberen_US
dc.contributor.advisorDaniel Feldheim, Committee Memberen_US
dc.contributor.advisorJan Genzer, Committee Memberen_US
dc.contributor.authorBrewer, Scott Harmonen_US
dc.date.accessioned2010-04-02T19:15:10Z
dc.date.available2010-04-02T19:15:10Z
dc.date.issued2005-12-01en_US
dc.degree.disciplineChemistryen_US
dc.degree.leveldissertationen_US
dc.degree.namePhDen_US
dc.description.abstractA variety of experimental spectroscopic techniques complemented by theoretical calculations when appropriate were used to investigate DNA adlayers on surfaces and proteins in solution. The formation and characterization of DNA adlayers on gold and indium tin oxide surfaces were characterized along with subsequent surface DNA hybridization. Prior to the modification of indium tin oxide surfaces with DNA, the optical and electronic properties of this metal oxide, fluorine doped tin oxide and iridium oxide were investigated. The detection of DNA hybridization on indium tin oxide surfaces utilized gold nanoparticle labeled target ssDNA. Further work on gold surfaces was performed using infrared spectroscopy to detect sugar binding to a phenylboronic acid terminated self-assembled monolayer. The binding properties and stability of gold nanoparticles were investigated by characterizing citrate and bovine serum albumin binding to gold surfaces and the stability of particles stabilized by these molecules. The stability and folding kinetics of the three helix bundle protein, villin headpiece subdomain was also investigated in addition to a theoretical investigation of the vibrational Stark effect. Finally, a time resolved step scan FTIR spectrometer was implemented with five microsecond time resolution.en_US
dc.identifier.otheretd-11292004-160406en_US
dc.identifier.urihttp://www.lib.ncsu.edu/resolver/1840.16/5515
dc.rightsI hereby certify that, if appropriate, I have obtained and attached hereto a written permission statement from the owner(s) of each third party copyrighted matter to be included in my thesis, dissertation, or project report, allowing distribution as specified below. I certify that the version I submitted is the same as that approved by my advisory committee. I hereby grant to NC State University or its agents the non-exclusive license to archive and make accessible, under the conditions specified below, my thesis, dissertation, or project report in whole or in part in all forms of media, now or hereafter known. I retain all other ownership rights to the copyright of the thesis, dissertation or project report. I also retain the right to use in future works (such as articles or books) all or part of this thesis, dissertation, or project report.en_US
dc.subjectProtein Foldingen_US
dc.subjectFTIRen_US
dc.subjectTemperature-Jumpen_US
dc.subjectDNAen_US
dc.subjectDensity Functional Theoryen_US
dc.subjectITOen_US
dc.titleSolution and Surface Characterization of DNA and Proteinsen_US

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