Polymer crowders and protein crowders act similarly on protein folding stability.
Recently a polymer crowder and two protein crowders were found to have opposite effects on the folding stability of chymotrypsin inhibitor 2 (CI2), suggesting that they interact differently with CI2. Here we propose that all the macromolecular crowders act similarly, with an entropic component favoring the folded state and an enthalpic component favoring the unfolded state. The net effect is destabilizing below a crossover temperature but stabilizing above it. This general trend is indeed observed in recent experiments and hints experimental temperature as a reason for the opposite crowding effects of the polymer and protein crowders.
Department of Physics and Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306, USA. hzhou4@fsu.edu
Huan-Xiang
HX
Zhou
D000465:Algorithms; D000818:Animals; D002417:Cattle; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry*; D011205:Povidone / Q000737:chemistry*; D017510:Protein Folding; D055550:Protein Stability; D017434:Protein Structure, Tertiary; D012710:Serum Albumin, Bovine / Q000737:chemistry; D013816:Thermodynamics
D010455:Peptides; D010940:Plant Proteins; C093336:chymotrypsin inhibitor 2; D012710:Serum Albumin, Bovine; D011205:Povidone