Date of Presentation
4-23-2024 9:00 AM
College
College of Science & Mathematics
Faculty Sponsor(s)
Dr. Gregory A. Caputo
Poster Abstract
Myoglobin, a widely studied protein in biophysics, is a small, helical, and highly soluble protein that has been investigated for decades. Its heme prosthetic group facilitates easy analysis of its folding state through absorbance spectroscopy. Ionic liquids (ILs), particularly room-temperature ionic liquids or molten salts, have gained significant attention in the past 15- 20 years for their potential use in electrochemical devices. Recently, their biocompatibility has become a focal point in research, given that certain IL species can either stabilize or destabilize biomolecular structures. This study employs absorbance and fluorescence spectroscopy to examine how amino acid-based ILs, specifically tetramethyl guanidine and choline as cations and serine, aspartic acid, and proline as anions, impact the unfolding of myoglobin. These amino acids were chosen based on previous findings indicating their varying effects on the protein azurin. The study evaluates the individual impacts of these amino acids and their collective ability to destabilize lysozyme when denatured with guanidinium HCl, monitored through absorbance spectroscopy and fluorescence signals from the heme group, Trp fluorescence, and Trp-heme interactions.
Student Keywords
Myoglobin Unfolding, Protein Stability, TMG
Disciplines
Chemistry
Document Type
Poster
Included in
Myoglobin Unfolding and Protein Stability With TMG
Myoglobin, a widely studied protein in biophysics, is a small, helical, and highly soluble protein that has been investigated for decades. Its heme prosthetic group facilitates easy analysis of its folding state through absorbance spectroscopy. Ionic liquids (ILs), particularly room-temperature ionic liquids or molten salts, have gained significant attention in the past 15- 20 years for their potential use in electrochemical devices. Recently, their biocompatibility has become a focal point in research, given that certain IL species can either stabilize or destabilize biomolecular structures. This study employs absorbance and fluorescence spectroscopy to examine how amino acid-based ILs, specifically tetramethyl guanidine and choline as cations and serine, aspartic acid, and proline as anions, impact the unfolding of myoglobin. These amino acids were chosen based on previous findings indicating their varying effects on the protein azurin. The study evaluates the individual impacts of these amino acids and their collective ability to destabilize lysozyme when denatured with guanidinium HCl, monitored through absorbance spectroscopy and fluorescence signals from the heme group, Trp fluorescence, and Trp-heme interactions.