(589d) How the Solvation of Flexible Solutes Influences Their Conformations

Patel, A., University of Pennsylvania
Jiang, Z., University of Pennsylvania
Dhabal, D., University of Pennsylvania
Under ambient conditions, globular proteins fold into well-defined “native” states, which are stabilized in part by a reduction in unfavorable protein-water interactions. Under a variety of conditions, such as lower temperatures, higher pressures, proximity to hydrophobic interfaces, and the presence of certain co-solutes, which modulate protein-water interactions, proteins can be unfolded or denatured resulting in a loss of their function. Using hydrophobic polymers as model globular proteins, here we study how the hydration environment of a polymer influences the thermodynamics of its collapse / folding transition. We find that near ambient conditions, typical hydrophobic macromolecules are situated at the edge of a collective collapse transition, making them particularly sensitive to perturbations such as the application of pressure or the presence of co-solutes.