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Isothermal Titration Calorimetry Studies Of Protein-Mediated Interactions And Preliminary Structural Studies Of Tandem Pdz1-2 Domain Of Psd-95 Protein, Ana Jankovic
Wayne State University Dissertations
Protein-mediated interactions that involve multiple ligands in their binding mechanisms are critical for many cellular functions. The primary focus of this dissertation research was to investigate such interactions for two proteins, the PDZ domain and frataxin, involving peptide and metal binding ligands, respectively. The three component projects of this work comprised (1) thermodynamic analysis of PDZ domain binding using calorimetry; (2) X-ray crystallographic structural studies of a PDZ dual domain; and (3) thermodynamic analysis of frataxin binding to iron. The specific goal of the research conducted with the PDZ domains was to understand the mechanism of action of multiple/tandem protein …
Computational Modeling Studies Of The Structures And Properties Of Organotin(Iv) And Stannyl-Thioether Systems With Comparisons To X-Ray Crystallography, Michelle R. Stem Joseph
Computational Modeling Studies Of The Structures And Properties Of Organotin(Iv) And Stannyl-Thioether Systems With Comparisons To X-Ray Crystallography, Michelle R. Stem Joseph
Open Access Theses & Dissertations
Controlling the toxic effects of organotin(IV) compounds involves engineering the structure of the molecules to optimize their properties. Molecular engineering, coupled with improved capabilities to generate reliable computational optimization models (COMs), will enable researchers to have greater success at harnessing the highly specific cytotoxicity of organotins. For example, as the thion ligand phenyl groups were replaced with Cl atoms, the S-Sn intramolecularity was strengthened, the bond distance decreased, and the stannyl tetrahedral structure was deformed from its triphenyl conformation. With each substitution, conformation deformations lowered the damaging bioactivity levels of thion. Bonding various ligands to organotin(IV) compounds …