title: Protein crowding tunes protein stability.
abstract: Thirty percent of a cell's volume is filled with macromolecules, and protein chemistry in a crowded environment is predicted to differ from that in dilute solution. We quantified the effect of crowding by globular proteins on the equilibrium thermodynamic stability of a small globular protein. Theory has long predicted that crowding should stabilize proteins, and experiments using synthetic polymers as crowders show such stabilizing effects. We find that protein crowders can be mildly destabilizing. The destabilization arises from a competition between stabilizing excluded-volume effects and destabilizing nonspecific interactions, including electrostatic interactions. This competition results in tunable stability, which could impact our understanding of the spatial and temporal roles of proteins in living systems.
authors.affiliation: Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA.
authors.forename: Andrew C
authors.initials: AC
authors.lastname: Miklos
authors.forename: Mohona
authors.initials: M
authors.lastname: Sarkar
authors.forename: Yaqiang
authors.initials: Y
authors.lastname: Wang
authors.forename: Gary J
authors.initials: GJ
authors.lastname: Pielak
mesh_terms: D009113:Muramidase / Q000737:chemistry; D011205:Povidone / Q000737:chemistry; D011487:Protein Conformation; D017510:Protein Folding; D055550:Protein Stability; D012710:Serum Albumin, Bovine / Q000737:chemistry; D012996:Solutions; D055672:Static Electricity
chemical_list: D012996:Solutions; D012710:Serum Albumin, Bovine; C421864:hen egg lysozyme; D009113:Muramidase; D011205:Povidone