The crowded and complex environment in cells is predicted to affect protein behavior compared to dilute buffer. My laboratory and our collaborators are examining how crowding affects the stability of proteins and their complexes in cells and under physiologically relevant crowded conditions using NMR. A challenge in these endeavors is detecting the test protein in a sea of crowders. NMR is ideally suited to overcome this challenge and provide high quality data on folded- and unfolded- proteins as well as free and bound forms of complexes. I will focus on equilibrium data acquired in living Escherichia coli cells, Xenopus laevis and Danio rerio oocytes as well as in vitro in concentrated cosolute solutions. The cosolutes include synthetic polymers and their monomers, other proteins and lyophilized cytosol. The results show that crowding affects folding and binding in ways not always correctly predicted by simple theory. The differences point to opportunities for theoretical efforts and simulations.

Protein- & protein- complex stability in living cells

Fall 2022 abstracts, posters, and presentations will launch in mid-September.

ACS Fall 2022

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.