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Full-Text Articles in Physical Sciences and Mathematics
A Systematic Investigation Of The Effects Of Chain Length And Ionic Head Group On Perfluoroalkyl Acid Binding To Human Serum Albumin, Jake Ulrich
Honors Theses
Perfluoroalkyl acids (PFAAs) are industrial chemicals used in everyday products ranging from non-stick coatings to fire-fighting foam. PFAAs are contaminants of emerging concern (CECs) and are bioaccumulative, persistent and toxic. Unlike other CECs, PFAAs bioaccumulate in areas of high protein concentration, such as the kidneys, liver and blood; therefore, it is vital to study PFAA-protein interactions. Human Serum Albumin (HSA) is the model protein used for PFAA-protein studies because it is the most abundant protein in the human body and it binds and transports endogenous and exogenous ligands. Previously, researchers have investigated PFAA-HSA binding, but most of these studies have …
Network Exploration Of Correlated Multivariate Protein Data For Alzheimer's Disease Association, Matthew J. Lane
Network Exploration Of Correlated Multivariate Protein Data For Alzheimer's Disease Association, Matthew J. Lane
Theses
Alzheimer Disease (AD) is difficult to diagnose by using genetic testing or other traditional methods. Unlike diseases with simple genetic risk components, there exists no single marker determining as to whether someone will develop AD. Furthermore, AD is highly heterogeneous and different subgroups of individuals develop the disease due to differing factors. Traditional diagnostic methods using perceivable cognitive deficiencies are often too little too late due to the brain having suffered damage from decades of disease progression. In order to observe AD at early stages prior to the observation of cognitive deficiencies, biomarkers with greater accuracy are required. By using …
Mutagenic And Spectroscopic Investigation Of Ph Dependent Cooa Dna Binding, Brian R. Weaver
Mutagenic And Spectroscopic Investigation Of Ph Dependent Cooa Dna Binding, Brian R. Weaver
Chemistry Honors Papers
The carbon monoxide (CO) sensing heme protein, CooA, is a transcription factor which exists in several bacteria that utilize CO as an energy source. CooA positively regulates the expression of coo genes in the presence of CO such that the corresponding proteins may metabolize CO. The present studies have yielded the unexpected result that Fe(III) CooA binds DNA tightly at pH < 7, deviating from all previously reported work which indicate that CooA DNA binding is initiated only when the exogenous CO effector reacts with the Fe(II) CooA heme. This observation suggests that the disruption of one or more salt bridges upon effector binding may be a critical feature of the normal CooA activation mechanism. To test this possibility, several protein variants that eliminated a selected salt bridge for the CooA homolog from Rhodospirillum rubrum were prepared via site-directed mutagenesis. Samples of these variant proteins, which were overexpressed in Escherichia coli, were then characterized by spectroscopic methods and functional assays to investigate the impact these mutations had on CooA heme coordination …