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Item Effect of monomeric binding affinity on scaffold mediated protein aggregation(Montana State University - Bozeman, College of Letters & Science, 2015) Goodman, Candace Kay; Chairperson, Graduate Committee: Mary J. CloningerThe intermolecular interactions that occur in a system determine the degree and duration of the contact. They govern processes from signaling and recognition to aggregation and tumor formation. The ability to control and affect intermolecular processes requires an understanding of the assembly process and factors modulating the assembly, such as the strength of individual interactions (binding affinity) and the number of interactions between molecules (valency). Functionalized PAMAM dendrimers were used as nucleating scaffolds to study the significance of intermolecular interactions on aggregate assembly. Dendrimers functionalized with biotin, lactose and mannose units spontaneously aggregated when added to the appropriate protein binding partner (streptavidin, galectin-3, and Concanavalin A, respectively). Aggregates were characterized to provide insight regarding the effects of binding affinity, protein valency and concentration on the average diameter, regularity (polydispersity) and kinetics of aggregate formation. A number of tools were used in this investigation, including dynamic light scattering (DLS), fluorescence microscopy (FM) and fluorescence lifetime spectroscopy (FLS). FLS instrumentation was reconfigured to enable high thoughput formats. A discussion of the validation and re-design of the FLS instrumentation is included.Item Characterization of 1La and 1Lb emission from indole-polar solvent complexes by supersonic jet spectroscopy(Montana State University - Bozeman, College of Letters & Science, 1999) Short, Kurt WilliamItem Excited state lifetimes of pyrimidines and purines in room temperature solution from fluorescence quantum yields and anisotropies(Montana State University - Bozeman, College of Letters & Science, 1980) Knighton, Walter BerkettItem Two photon study of environmental effects on indole spectra(Montana State University - Bozeman, College of Letters & Science, 1990) Rehms, Aden AndrewItem Solvent effects on the electronic spectra of indoles : theoretical methods and laser induced fluorescence excitation in supersonic jet(Montana State University - Bozeman, College of Letters & Science, 1993) Muino Montero, Pedro LuisItem Polarized one- and two-photon fluorescence excitation spectroscopy on selected nucleic acid bases(Montana State University - Bozeman, College of Letters & Science, 1989) Williams, Scott AllanItem The methyl rotor as a probe of electronic character via fluorescence excitation of para-substituted toluenes(Montana State University - Bozeman, College of Letters & Science, 1990) Mayer, Steven GregoryItem Polarized two-photon fluorescence excitation studies of jet-cooled indoles(Montana State University - Bozeman, College of Letters & Science, 1992) Sammeth, David MichaelItem Design and synthesis of fluorescent dyes for use in proteomic research(Montana State University - Bozeman, College of Letters & Science, 2008) Spicka, Kevin James; Chairperson, Graduate Committee: Paul Grieco; Hien Hguyen (co-chair)Proteomics is a rapidly developing field requiring powerful new technology in order to be able to detect proteins at increasingly lower concentrations. To aid in the detection of proteins at lower concentrations, DIGE dyes, a family of spectrally resolved fluorescent dyes, are currently available to proteomic researchers for 2D gel analysis. However, the demands of protein detection dictate that dyes that are even more sensitive and versatile be created. The syntheses of highly sensitive, water soluble BODIPY fluorophore dyes are described. These dyes are proposed to have the necessary sensitivity to allow for detection of proteins in much lower concentrations, providing an improvement over current protein detection limits. The BODIPY dyes that have been synthesized are available in a variety of absorbances and emissions. While fluorescent dyes that are amine-reactive are the most popular covalently binding protein labeling markers being used in today's proteomic research, thiol-reactive fluorescent markers are gaining importance in proteomic research. Since thiol residues are less common in proteins compared to their amine counterparts, saturation labeling and quantification are more easily achieved. The syntheses of sensitive thiol- reactive fluorescent dyes are described. These syntheses allow for quick generation of thiol-reactive fluorescent markers to be used in proteomic research.