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Full-Text Articles in Physical Sciences and Mathematics
Characterization Of Glycation Sites On Human Serum Albumin Using Mass Spectrometry, Omar S. Barnaby
Characterization Of Glycation Sites On Human Serum Albumin Using Mass Spectrometry, Omar S. Barnaby
Department of Chemistry: Dissertations, Theses, and Student Research
The modification of proteins by reducing sugars is a process that occurs naturally in the body. This process, which is known as glycation, has been linked to many of the chronic complications encountered during diabetes. Glycation has also been linked to changes in the binding of human serum albumin (HSA) to several drugs and small solutes in the body. While these effects are known, there is little information that explains why these changes in binding occur. The goal of this project was to obtain qualitative and quantitative information about glycation that occurs on HSA. The first section of this dissertation …
Evidence For Specific Subunit Distribution And Interactions In The Quaternary Structure Of Α-Crystallin, Amie M. Morris, J. Andrew Aquilina
Evidence For Specific Subunit Distribution And Interactions In The Quaternary Structure Of Α-Crystallin, Amie M. Morris, J. Andrew Aquilina
Faculty of Science - Papers (Archive)
The quaternary structure of α-crystallin is dynamic, a property which has thwarted crystallographic efforts towards structural characterization. In this study, we have used collision-induced dissociation mass spectrometry to examine the architecture of the polydisperse assemblies of α-crystallin. For total α-crystallin isolated directly from fetal calf lens using size-based chromatography, the αB-crystallin subunit was found to be preferentially dissociated from the oligomers, despite being significantly less abundant overall than the αA-crystallin subunits. Furthermore, upon mixing molar equivalents of purified αA- and αB-crystallin, the levels of their dissociation were found to decrease and increase, respectively, with time. Interestingly though, dissociation of subunits …
The Path To Preservation: Using Proteomics To Decipher The Fate Of Diatom Proteins During Microbial Degradation, Brook L. Nunn, Ying S. Ting, Lars Malmström, Yihsuan S. Tsai, Angela Aquier, David R. Goodlett, H. Rodger Harvey
The Path To Preservation: Using Proteomics To Decipher The Fate Of Diatom Proteins During Microbial Degradation, Brook L. Nunn, Ying S. Ting, Lars Malmström, Yihsuan S. Tsai, Angela Aquier, David R. Goodlett, H. Rodger Harvey
OES Faculty Publications
We drew upon recent advances in tandem mass spectrometry-based proteomic analyses in order to examine the proteins that remain after a diatom bloom enters the stationary phase, precipitates out of the photic zone, and is subjected to microbial degradation over a 23-d period within a controlled laboratory environment. Proteins were identified from tandem mass spectra searched against three different protein databases in order to track proteins from Thalassiosira pseudonana and any potential bacterial contributions. A rapid loss of diatom protein was observed over the incubation period; 75% of the proteins initially identified were not detected after 72 h of exposure …