Life Sciences Commons^™

Coomassie Brilliant Blue Dye As A Method For Analyzing Fracture Markings In Bone, Abigail Hoffmeister, David Harutunyan, Matthew Aizawa, Everett Baker, Brandon Mendoza, Chase Freeman, Siran Iskanian

Seaver College Research And Scholarly Achievement Symposium

Coomassie Brilliant Blue Dye is a dye commonly used to stain proteins. Because of its ability to adhere to proteins, this research has focused on perfecting a method of dyeing a fractured flat bone in order to most accurately observe and analyze fracture markings within the trabecular layer. Stereoscopic microscopy was the chosen technique of analysis for this research because of its proven effectiveness in glass and ceramic fractography to observe varying depths. In order to most effectively apply stereoscopic microscopy to this research, the following variables were manipulated to maximize color contrast in the trabecular layer in order to …

Mediation Of The Uncoupled Enos Pathway Following Oxidative Stress Using Tetrahydrobiopterin And Nitric Oxide Donor Drugs To Restore Tetrahydrobiopterin Concentration, Brianna Munnich

Scholar Week 2016 - present

Presentation Location: Warming House, Olivet Nazarene University

Abstract

The eNOS pathway, found in the endothelium of blood vessels, is a key regulator of nitric oxide levels in the circulatory system. The pathway is controlled through several positive and negative feedback loops [2]. The cofactor tetrahydrobiopterin (BH4) is a major control point in this pathway and under conditions of stress can be reduced into the dihydrobiopterin (BH2) [2,6,7,8,9]. When the reduced form is predominant, the pathway produces reactive oxygen species (ROS) rather than nitric oxide, causing stress and damage to the vessels [6,7,8,9]. In this study, different treatments were studied …

Probing Large Intrinsically Disordered Regions Through Novel Sortase-Mediated Ligation, Leah Kjormoe

Scholars Week

In the realm of proteins, it is widely accepted that structure informs function. However, there are many proteins that contain intrinsically disordered regions (IDRs). These regions are areas in which the protein lacks defined structure, and IDPs are also often unstable, which complicates structural studies. NMR spectroscopy is an established method for probing protein structure and has been applied to that end in small IDRs. However, larger IDRs often have spectral overlap that makes data difficult to interpret. Furthermore, low-concentration samples limit spectral clarity. One method to address these difficulties is to use sortase ligation and segmental labeling, which increases …

Site-Directed Mutagenesis Of Malate Dehydrogenase: A Class Project, Bruce J. Heyen, Chesley Rowlett, Jon Zatorski, Ryan Burch, Emily Veach, Andy Gemmaka

Scholar Week 2016 - present

Malate dehydrogenase (MDH) is an important enzyme in an organism’s metabolic pathways. MDH is found in almost all living cells and catalyzes the conversion of malate to oxaloacetate which also involves nicotinamide dehydrogenase (NAD) as a coenzyme. A method to study how an enzyme operates is to alter one of its amino acids and compare the activity of the enzyme before and after the mutation. As a class project in Advanced Biochemistry during the spring semester of 2018, we are working as a team to propose and carry out a point-based mutation on MDH.

Synthesis And Incorporation Of 1,2-Alkanolamine-Functionalized Lysine As A Non-Canonical Amino Acid Into Gfp, Chesley M. Rowlett

Scholar Week 2016 - present

Synthesis of specific post translational modifications in proteins can be difficult but achievable via genetic code expansion techniques. An attempt has been made to synthesize and incorporate D-cThrK into green fluorescent protein (GFP) at an amber mutation site in Escherichia coli via the coordination of pyrrolysyl- tRNA synthetase and its cognate tRNApyl. The incorporation of this non-canonical amino acid and potential chemical transformations following it allow the synthesis of proteins with post translational lysine modifications, making a variety of basic and biotechnological applications available.

Using Fluorescence Microscopy To Identify A Potential New Treatment For Heart Failure, Ryan D. Himes

Scholar Week 2016 - present

Cardiac glycosides have been used to treat heart failure for centuries, but they have a narrow therapeutic window, as they inhibit their target receptor nearly irreversibly. Overdoses can lead to arrhythmias. Phospholemman is a natural inhibitor of the same target as cardiac glycosides. It is possible that mutating phospholemman could achieve the same therapeutic benefit, while allowing cells to reverse the inhibition and thereby avoid an arrhythmia. I used fluorescence microscopy to screen candidate phospholemman mutants and identify one that binds more avidly to its target than the naturally occurring phospholemman. This mutant, L30A, caused similar effects as cardiac glycosides …

Characterizing The Role Of Aif4 In Saccharomyces Cerevisiae, Antonia L. Hur Ms., Nina Serratore Ms., Scott D. Briggs

The Summer Undergraduate Research Fellowship (SURF) Symposium

Chromatin remodelers are important regulatory mechanisms that eukaryotic cells use to modify the structure of chromatin, which is made up of DNA and proteins. DNA wraps around histone proteins to make up chromatin. When these proteins are modified, the shape of the chromatin is altered. “Loosening” the chromatin structure by chromatin modifications allows for active gene expression whereas “tightening” or compaction of chromatin results in gene repression. Therefore the modifications on chromatin modulate gene expression in all eukaryotes. It has been shown that mis-regulation of chromatin remodelers contribute to various cancers. Understanding the biochemistry behind how chromatin associating proteins modify …