Sánchez Díaz, Luis Enrique
University of Tennessee at Chattanooga
Place of Publication
Apopliprotein or ApoA-1 is a complex lipoprotein that functions in the removal of cholesterol from the blood, removing cholesterol from the area around white blood cells and promoting the excretion of lipids through the lymphatic system. Previous research has found that ApoA-1 shows both folded and unfolded conformations depending on the concentration of NaCl in solution in the water around it. The protein was studied using molecular dynamics simulations. Once this state of equilibrium was reached, various structural properties of the protein were measured including the radius of gyration and the radial distribution function. The goal of the project was to determine if ApoA-1 had stable folding conformations in various concentrations of Potassium Chloride and how those concentrations compared with the concentration of Sodium Chloride around known stable conformations. Previous research has determined that in a range of concentrations from 0.5M to 2.0M ApoA-1 has both folded and unfolded conformations. We are now working to study Potassium Chloride in these concentrations to determine if the radius of gyration results will be the same as the ones found in studying the sodium chloride. This research will determine if the healthier salt potassium chloride, allows for the same folded and stable conformations of ApoA-1.
Dr. Luis-Sanchez Diaz, Dr. Josh Hamblen
B. S.; An honors thesis submitted to the faculty of the University of Tennessee at Chattanooga in partial fulfillment of the requirements of the degree of Bachelor of Science.
Apolipoproteins; Molecular dynamics; Protein folding
Biochemistry | Physical Chemistry
Holmberg, Hannah, "Molecular dynamic simulation of the complex folding patterns of Apolipoprotein A1 in various concentrations of potassium chloride" (2021). Honors Theses.