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Full-Text Articles in Physical Sciences and Mathematics
Insights Into Chemical Structure Changes Of Kerogen From Bituminous Coal In Response To Dike Intrusions Investigated By Advanced Solid-State 13C Nmr, Yuan Li
Chemistry & Biochemistry Theses & Dissertations
Variations in the chemical structures of kerogens From highly volatile bituminous coal located near two igneous dike intrusions in the Illinois Basin were examined in detail by advanced solid-state 13C nuclear magnetic resonance (NMR) spectroscopy. Spectral-editing techniques were used to identify specific functional groups. Direct polarization was used to quantify different functional groups. 1H-13C two- dimensional heteronuclear NMR was used to examine connectivities and proximities, and 1H-13C long-range recoupled dipolar dephasing was used to estimate aromatic cluster sizes. With decreasing distance to dike contacts and increasing thermal maturity (vitrinite reflectance R0 from …
In-Cell And In Vitro Studies Of Disease Related Protein-Protein Interactions Using Nmr-Spectroscopy, Andres Yudiel Maldonado
In-Cell And In Vitro Studies Of Disease Related Protein-Protein Interactions Using Nmr-Spectroscopy, Andres Yudiel Maldonado
Legacy Theses & Dissertations (2009 - 2024)
The receptor for advanced glycation end products (RAGE) is a multiligand cell surface macromolecule that plays a central role in the etiology of diabetes, inflammation, and neurodegeneration. The cytoplasmic domain of RAGE, ctRAGE, is critical for RAGE-dependent signal transduction. As the most membrane proximal event, mDia1 binds to ctRAGE and is essential for RAGE ligand-stimulated phosphorylation of AKT and cell proliferation/migration. We show that ctRAGE contains an unusual alpha-turn that mediates the mDia1-ctRAGE interaction and is required for RAGE dependent signaling. The results establish a novel mechanism through which an extracellular signal initiated by RAGE ligands regulates RAGE signaling in …
Structural Interactions And Dynamics Of Disease Related Proteins By Using Nmr Spectroscopy, Shadakshara Swamy Puttamadappa
Structural Interactions And Dynamics Of Disease Related Proteins By Using Nmr Spectroscopy, Shadakshara Swamy Puttamadappa
Legacy Theses & Dissertations (2009 - 2024)
Nuclear Magnetic Resonance (NMR) is a powerful spectroscopic technique to study the structure, molecular interactions, and dynamics of proteins. Modern NMR instrumentation, advancements in experimental techniques and revolutionary developments in recombinant DNA technology have made NMR a versatile and very convenient tool for biomolecule characterization.