Resolving the enthalpy of protein stabilization by macromolecular crowding.

ABSTRACT: Proteins in the cellular milieu reside in environments crowded by macromolecules and other solutes. Although crowding can significantly impact the protein folded state stability, most experiments are conducted in dilute buffered solutions. To resolve the effect of crowding on protein stability, we use ¹⁹ F nuclear magnetic resonance spectroscopy to follow the reversible, two-state unfolding thermodynamics of the N-terminal Src homology 3 domain of the Drosophila signal transduction protein drk in the presence of polyethylene glycols (PEGs) of various molecular weights and concentrations. Contrary to most current theories of crowding that emphasize steric protein-crowder interactions as the main driving force for entropically favored stabilization, our experiments show that PEG s

SUBMITTER: Stewart CJ 

PROVIDER: S-EPMC9942490 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature