The general area our lab researches is organic chemistry. The purpose of our research is to create a foldamer capable of switching on in the presence of a chemical fuel. A foldamer is a discrete chain molecule that folds into a conformationally ordered state in solution. They are artificial molecules that mimic the ability of […]
A39: Do Charged Residues in Grp94 Facilitate Client Binding: Insights into Chaperone Function
The Hsp90 family of chaperones functions to target misfolded proteins, prevent aggregate formation and bind to specific substrates for proper folding. Paralogs of the Hsp90 family exist in the cytoplasm (Hsp90), in the mitochondria (TRAP1) and in the endoplasmic reticulum (Grp94). The ER paralog Grp94 is of particular interest to this investigation since it is […]
A36: Heart Membrane Proteins’ Malfunction Leads to Long- QT Syndrome: Detergent Free Purification of KCNE1 Using Functionalized SMALPS
KCNE1 and KCNQ1 are membrane proteins located in the heart that are responsible for repolarization. Malfunction of these proteins can lead to “Long QT Syndrome”—a condition that can cause life threatening arrhythmia and sudden cardiac death. Styrene maleic acid copolymer lipid nanoparticles (SMALPS) is a membrane mimetic system that purifies a protein and allows for […]
A37: Investigating A Novel Family Of Proteins in Ancient Cyanobacteria
We investigate a family of proteins called pentapeptide repeat proteins in attempt to solve their structures and functions within cyanobacteria. We attempt to solve protein structures through protein X-ray crystallography and attempt to solve the function of our proteins through various methods including generating growth curves, filament length distributions, monitoring heterocyst formation frequencies and patterns, […]
C12: The role of lipids in thylakoid protein insertion
Most photosynthetic proteins are synthesized in the cytoplasm of the plant cell but are used in the thylakoid membrane of the chloroplast. The cpTAT pathway is a transport pathway in the thylakoid that helps move photosynthesis-related proteins to their site of function and requires the work of three membrane proteins, Tha4, Hcf106, and cpTatC. Membranes, […]
C22: Refining the Structural Topology of S21 Pinholin in a Lipid Bilayer Via Electron Paramagnetic Resonance
Membrane proteins are often used as targets for development of new drugs. Unfortunately, it is often difficult to determine the structures of these membrane proteins in their native environment due to hydrophobic interactions. It is estimated that 25% of all proteins are membrane proteins, yet structures have only been solved for a few hundred. Holins […]
A13: Over Expressing and Purifying Proteins
Purity is a measurement used to describe a wide variety of things from jewelry, to drinking water. Purity is also involved in biochemistry, specifically when studying the behavior of biological mechanisms. The mechanism of interest for the Dabney-Smith lab is the twin-arginine translocation (Tat) pathway that moves proteins around the cell. To effectively study this […]
A12: Investigation of Effects of Salicylic Acid on Mitochondrial TatC Expression in Arabidopsis thaliana
The Twin Arginine Translocation pathway (TAT) is a protein pathway that is fueled only by the proton motive force, can transport fully folded proteins, and is present in bacteria, archaea and eukaryotic organelles such as the chloroplast and mitochondria. It is well known as to the function of this pathway in bacteria and chloroplasts, though […]
B21: Evolutionary Mechanism of Antibiotic Resistance: VIM – 4 Metallo-β-lactamases
Metallo-β-lactamases (MBLs) are a class of proteins contributing to the ongoing but often unrecognized antibiotic resistance crisis, in which many current and most past antibiotics are less effective than when first introduced. These proteins protect bacteria by destroying manmade antibiotics, and have spread worldwide in part due to the selective pressure of antibiotic overprescription. To […]
A19: Functional and physical interaction between Hsp90 and Hsp70
Heat shock protein 90 (Hsp90) is an extremely abundant molecular chaperone. Hsp90 has roles in the folding and reactivation of hundreds of client proteins. Chaperones like Hsp90 complete their protein remodeling activities using energy generated from ATP hydrolysis. To complete the protein folding process, Hsp90 collaborates with many other co-chaperones, including the Hsp70 chaperone system. […]
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