Chemistry Commons^™

Probing Small Heat Shock Protein Chaperoning Activity Through The Interaction Between Myoglobin And Guanidine Hydrochloride, Jacob Mcdowell

Celebration of Research

Myoglobin is a small biological protein found in most muscle tissues. When in the proper form (native/folded), myoglobin can serve its primary function: binding oxygen. However, like all proteins, myoglobin can denature through a variety of processes into a form that no longer binds oxygen. One denaturant, guanidine hydrochloride (GuHCl), is the biological product of protein metabolism. Another class of biological proteins is small heat shock proteins (sHSPs), which have the function of chaperoning other proteins to prevent the denaturing process. Previously, in physical chemistry lab, we explored the GuHCl-induced denaturing of myoglobin. Former Northwestern students used fluorescence correlation spectroscopy …