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Full-Text Articles in Chemistry
2-D Electrophoresis Modeling Of Multienzyme Cutting Of Polypeptides, Howard Mayes
2-D Electrophoresis Modeling Of Multienzyme Cutting Of Polypeptides, Howard Mayes
Theses
2-Dimensional Electrophoresis is one of the tools in the identification of proteins by molecular weight and pH. The display of molecular weight allows the researcher to quickly identify whether a specific protein or peptide string is in the sample. The pH measurement allows even better resolution between different species in the sample. The MultiEnzyme ElectroPhoresis (MEEP) program tries to model that by providing a graph that displays separated protein strings by both molecular weight and pH. The ability to cleave the protein with 43 different enzyme variations allows the researcher to analyze appropriate enzymes to isolate a protein subsequence before …
Structural And Functional Studies Of Proteins From The Agricultural Pests Tetranychus Urticae And Aspergillus Fumigatus, Caleb Schlachter
Structural And Functional Studies Of Proteins From The Agricultural Pests Tetranychus Urticae And Aspergillus Fumigatus, Caleb Schlachter
Theses and Dissertations
Agricultural pests are a worldwide problem and cause billions of dollars in crop loss. In the United States alone, an estimated $40 billion USD is lost per year due to insecticide resistance [1]. Studied here are proteins (potentially new pesticide targets) from the agricultural pests Tetranychus urticae and Aspergillus fumigatus. T. urticae, or twospotted spidermite, is a polyphagous pest, and three proteins from this pest, a cyanase, a glutathione S-transferase and an intradiol ring-cleavage dioxygenase are described [2]. Cyanase is involved in the conversion of bicarbonate and cyanate, a toxic self-defense metabolite produced by plants, into ammonia and carbon dioxide. …
Study Of Biologically Important Macromolecules By Nuclear Magnetic Resonance, Christopher Michael Demott
Study Of Biologically Important Macromolecules By Nuclear Magnetic Resonance, Christopher Michael Demott
Legacy Theses & Dissertations (2009 - 2024)
Intrinsically disordered proteins or unstructured segments within proteins play an important role in cellular physiology and pathology. A combination of peptide aptamers selected by using the yeast-two-hybrid scheme, and in-cell NMR identified high affinity binders to a transiently structured intrinsically disordered proteins (IDP). This method was validated using the prokaryotic ubiquitin-like protein, Pup, of the Mycobacterium proteasome. We discover two peptide aptamers that bind to opposite sites of a transient helix in Pup, an intrinsically disordered protein, that have vastly different effects on the survival of Mycobacterium bovis BCG.