Sürdürülebilir Yeşil Kampüs Koleksiyonu / Sustainable Green Campus Collection
Permanent URI for this collectionhttps://hdl.handle.net/11147/7755
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Doctoral Thesis Proteomic Studies and Its Application To Biological Samples Using Mass Spectrometry(Izmir Institute of Technology, 2017) Güray, Melda Zeynep; Yalçın, Talat; Karakaya, Hüseyin ÇağlarMass spectrometry (MS) is a powerful analytical tool with its application in the field of biological sciences for identification of proteins, defining post-translational modifications, studying protein expression and protein interactions. This thesis presents MS analyses of proteins for defining modifications observed during sample preparation and identification of proteins isolated from clinical samples and microorganisms. The first part of the thesis includes proteomic analysis of antimony resistant L. tropica. The results clearly indicated that the generation of antimony resistance by parasites, either in host organism or in vitro, causes alteration of protein expression levels, and the mechanism of antimony resistance in host organism and in vitro conditions follow different strategies. In the second part of the study, proteomic analysis of Bence Jones proteins isolated from urine of multiple myeloma patients was performed. Gel electrophoresis and MS analysis revealed that the proteins from different patients with different nephrotoxicity have different tendencies to form multimeric structures and contained different type of light chain. In the third part, it was shown that precipitation of proteins in acetone causes +98 u mass artifacts on proteins when analyzed by MS. The parameters affecting the formation of modification was studied and it was revealed that this modification is dependent on solution pH, incubation time and temperature. In the last part, aspartic acid and glutamic acid containing synthetic peptides were shown to be methylated upon incubation in acidified methanol solution. MS analysis revealed that the reaction is dependent on temperature and time and is affected by the type of acid included in methanol solution. All in all, this thesis provides a comprehensive study of proteins by mass spectrometry for identification of proteins from different sources, as well as defining protein modifications observed as artifacts during sample handling in proteomic workflows.Master Thesis Proteomic Analysis of Boron Stress Response in Yeast Saccharomyces Cerevisiale(Izmir Institute of Technology, 2011) Avşar, Kadir; Koç, AhmetBoron is a versatile element distributed in every part of the environment but most of its deposit reserves are localized in a few countries, Turkey being one of the most prominent. Boron is known to be an essential micronutrient for plants and some animals. Like any other essential element it has toxicity in high concentrations. Herein the mechanism of toxicity and the elements of the boron stress response were investigated in Saccharomyces cerevisiae with a proteomics approach. Boron is believed to have played a role in the evolution of life on earth. It has strongly electrophile organic compounds, the most important physiological form being boric acid. Boric acid has a capacity to bind cis-located hydroxl groups and some amino groups. Some of these groups are located at the active sites of some enzymes and at the carbohydrates with five-membered furanose rings. The riboses of some metabolically important molecules like S-adenosyl methionine, diadenosine phosphate family members and 3'end of RNAs are prone to be affected. The yeast cells subjected to boron in this study expressed higher amounts of carbohydrate metabolic enzymes, proteins involved in protein synthesis, protein folding and catabolism, redox homeostasis and nucleotide synthesis. All of these proteins are common to metal stress responses in yeasts. Some of them involve in other stress responses like peroxide, salt or herbicide stresses showing complex interplay between responses.