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Full-Text Articles in Physical Sciences and Mathematics
Nmr-Based And Automated Docking Characterization Of Protein Structure, Dynamics, And Ligand Binding, Andrew Lawrence Olson
Nmr-Based And Automated Docking Characterization Of Protein Structure, Dynamics, And Ligand Binding, Andrew Lawrence Olson
Dissertations (1934 -)
NMR-based methods used in conjunction with a technique called docking are used to characterize ligand binding to proteins. Standard NMR methods were used to study the backbone dynamics of substrate binding to phosphomevalonate kinase (PMK) and it was observed that ligand binding caused PMK to undergo large conformational changes. These changes were reflected by the appearance of many chemical shift changes upon binding of the natural substrates of PMK (both the binary and ternary complexes) in 1H-15N HSQC NMR titration experiments. The same process was used to characterize the effect ligand binding has on the many arginines in the active …
Design, Combinatorial Synthesis, And Biological Evaluation Of Novel Α-Helical Mimetics Based On Functionalized Piperazines As Antagonists Of P53/Mdm2 Interactions, Melissa Elizabeth Topper
Design, Combinatorial Synthesis, And Biological Evaluation Of Novel Α-Helical Mimetics Based On Functionalized Piperazines As Antagonists Of P53/Mdm2 Interactions, Melissa Elizabeth Topper
USF Tampa Graduate Theses and Dissertations
The p53 protein promotes tumor eradication upon activation, making it an attractive target in cancer therapies. A reported 50% of all human cancers display aberrant activation of the MDM2 oncoprotein, which directly promotes tumorgenesis by inactivating the transcriptional activity of wild type p53, and is commonly associated with drug, chemo, and radio therapy resistance. Previously reported crystallographic analysis of the p53/MDM2 complex infers that the p53 protein forms a 2.5 turn amphipathic alpha helix whose hydrophobic face interacts within a deep hydrophobic cleft in the NH2-terminal domain of the globular MDM2. This suggests that the synthesis of small molecular antagonists …
Electrochemical Behavior Of Kaempferide Interaction With Protein, Li-Qing Lin, Xin-Hua Lin, Jing-Hua Chen, Li-Ying Huang, Yin-Huan Liu, Guang-Wen Li
Electrochemical Behavior Of Kaempferide Interaction With Protein, Li-Qing Lin, Xin-Hua Lin, Jing-Hua Chen, Li-Ying Huang, Yin-Huan Liu, Guang-Wen Li
Journal of Electrochemistry
The electrochemical behavior of kaempferide at activated GCE and the interaction of kaempferide with human serum albumin( HSA) were investigated by cyclic voltammetry. A differential pulse voltammetric method has been proposed for the determination of the HSA with kaempferide. In pH 4. 5 phosphate buffer solutions ( PBS) kaempferide can react with HSA to form an electrochemically non-active supermolecular complex at activated GCE,resulting in the decrease of oxidation peak ( at 0. 468 V) without the change of peak potential. The decrease of the peak current is proportional to HSA concentration in the range of 0. 05 ～ 0. 25 …
Sorption Of Bovine Serum Albumin On Nano And Bulk Oxide Particles, Lei Song
Sorption Of Bovine Serum Albumin On Nano And Bulk Oxide Particles, Lei Song
Masters Theses 1911 - February 2014
Manufactured oxide nanoparticles (NPs) have large production and widespread applications, which will inevitably enter the environment. NPs can interact with proteins in living beings due to the fact that NPs can transport into blood or across cell membranes into cells. Conformational change of protein molecules after sorption on oxide NPs has been reported. Therefore, it is important to understand the adsorption mechanism of protein onto oxide NPs surfaces. Although few works have reported protein adsorption behaviors, a general systematic comparison of the effects of particle size and surface groups on protein adsorption by widely studied NPs still needs to be …
Elucidating The Structure Of Protein Aggregates By Raman Spectroscopy, Ludmila A. Popova
Elucidating The Structure Of Protein Aggregates By Raman Spectroscopy, Ludmila A. Popova
Legacy Theses & Dissertations (2009 - 2024)
The structures and properties of amyloid fibrils are of considerable interest due to their associations with numerous neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease and transmissible spongiform encephalopaties (prion diseases). Understanding fibrillogenesis at a molecular level requires detailed structural characterization of amyloid fibrils. However amyloid fibrils are difficult objects to study due to their non-crystalline and insoluble nature. These properties make the application of classical tools of structural biology, such as X-Ray crystallography and solution Nuclear Magnetic Resonance spectroscopy, impractical for structural characterization of protein fibrils.
Microfluidic Devices Interfaced To Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry For Proteomics, Jeonghoon Lee
Microfluidic Devices Interfaced To Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry For Proteomics, Jeonghoon Lee
LSU Doctoral Dissertations
Microfluidic interfaces were developed for off-line matrix-assisted laser desorption/ionization mass spectrometry (MALDI). Microfluidic interfaces allow samples to be manipulated on-chip and deposited onto a MALDI target plate for analysis. For this research, microfluidic culturing devices and automated digestion and deposition microfluidic chip platforms were developed for the identification of proteins. The microfluidic chip components were fabricated on a poly(methyl methacrylate), PMMA, wafer using the hot embossing method and a molding tool with structures prepared via micromilling. One of the most important components of the chip system was a trypsin microreactor. An open channel microreactor was constructed in a 100 µm …