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Incorporation Of Capillary-Channeled Polymer (C-Cp) Fibers Into Micropipette Tips For Solid Phase Extraction With Applications In Bioanalysis, Donald Fornea
All Theses
Solid phase extraction (SPE), is a widely used sample preparation method that is currently experiencing a surge in research interest, clever architecture/format development, and stationary phase characterization.1-3 SPE devices commonly exist in syringe, cartridge, disk, and micropipette tip formats.4 Micropipette tip SPE has enhanced the determination of proteins by electrospray ionization (ESI) and matrix assisted laser desorption ionization (MALDI) mass spectrometry (MS) by handling micro-liter volumes of sample and buffer removal/solvent exchange.5-7 Buffers have deleterious effects on ionization taking place in MS sources due to preferential ionization, ion suppression effects, and the formation of adduct species competing for ionization in …
Characterization Of Capillary-Channeled Polymer Fibers As Stationary Phases For High-Performance Liquid Chromatography Of Macromolecules, Dwella Nelson
All Dissertations
Capillary-channeled polymer (C-CP) fibers are being developed and characterized as high-performance liquid chromatography (HPLC) stationary phases for reversed-phase separations of proteins. Conventional porous phases are not well suited for separating large macromolecules due to the slow diffusivity of the molecules, large diffusional distances, and stagnant mobile phase zones within the column. Stationary phases are continually being developed to address the challenges associated with HPLC of proteins and other macromolecules in general. C-CP fiber stationary phases are an alternative to conventional bead technology and offer a variety of chemical and physical advantages. The fibers can be selected for their chemical functionality …
Development Of Polymer Monoliths For The Analysis Of Peptides And Proteins, Binghe Gu
Development Of Polymer Monoliths For The Analysis Of Peptides And Proteins, Binghe Gu
Theses and Dissertations
Several novel polymer monoliths for the analysis of peptides and proteins were synthesized using polyethylene glycol diacrylate (PEGDA) as crosslinker. Photo-initiated copolymerization of polyethylene glycol methyl ether acrylate and PEGDA yielded an inert monolith that could be used for size exclusion liquid chromatography of peptides and proteins. This macroscopically uniform monolith did not shrink or swell in either water or tetrahydrofuran. More importantly, it was found to resist adsorption of both acidic and basic proteins in aqueous buffer without any organic solvent additives. A strong cation-exchange polymer monolith was synthesized by copolymerization of 2-acrylamido-2-methyl-1-propanesulfonic acid (AMPS) and PEGDA. A ternary …
Capillary Electrophoresis Of Proteins With Selective On-Line Affinity Monoliths, Jenny Marcela Armenta Blanco
Capillary Electrophoresis Of Proteins With Selective On-Line Affinity Monoliths, Jenny Marcela Armenta Blanco
Theses and Dissertations
The analysis of proteins in biological fluids by capillary electrophoresis (CE) is of interest in clinical chemistry. However, due to low analyte concentrations and poor concentration limits of detection (CLOD), protein analysis by this technique is frequently challenging. Coupling preconcentration techniques with CE greatly improves the CLOD. An on-line preconcentration-CE method that can selectively preconcentrate any protein for which an antibody is available would be very useful for the analysis of low abundance proteins and would establish CE as a major tool in biomarker discovery. To accomplish this, an on-line protein G monolithic preconcentrator CE system for enrichment and separation …
Sequence-Specific Recognition And Cooperative Dimerization Of N-Terminal Aromatic Peptides In Aqueous Solution By A Synthetic Host, Lisa M. Heitmann, Alexander B. Taylor, P John Hart, Adam R. Urbach
Sequence-Specific Recognition And Cooperative Dimerization Of N-Terminal Aromatic Peptides In Aqueous Solution By A Synthetic Host, Lisa M. Heitmann, Alexander B. Taylor, P John Hart, Adam R. Urbach
Chemistry Faculty Research
This article describes the selective recognition and noncovalent dimerization of N-terminal aromatic peptides in aqueous solution by the synthetic host compound, cucurbit[8]uril (Q8). Q8 is known to bind two aromatic guests simultaneously and, in the presence of methyl viologen, to recognize N-terminal tryptophan over internal and C-terminal sequence isomers. Here, the binding of Q8 to aromatic peptides in the absence of methyl viologen was studied by isothermal titration calorimetry (ITC), 1H NMR spectroscopy, and X-ray crystallography. The peptides studied were of sequence X-Gly-Gly, Gly-X-Gly, and Gly-Gly-X (X = Trp, Phe, Tyr, and His). Q8 selectively binds and dimerizes Trp-Gly-Gly …
Optimization Of A Ribosomal Structural Domain By Natural Selection, Corina Maeder, G. L. Conn, D. E. Draper
Optimization Of A Ribosomal Structural Domain By Natural Selection, Corina Maeder, G. L. Conn, D. E. Draper
Chemistry Faculty Research
A conserved, independently folding domain in the large ribosomal subunit consists of 58 nt of rRNA and a single protein, L11. The tertiary structure of an rRNA fragment carrying the Escherichia coli sequence is marginally stable in vitro but can be substantially stabilized by mutations found in other organisms. To distinguish between possible reasons why natural selection has not evolved a more stable rRNA structure in E. coli, mutations affecting the rRNA tertiary structure were assessed for their in vitro effects on rRNA stability and L11 affinity (in the context of an rRNA fragment) or in vivo effects on cell …