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Polymer crowders and protein crowders act similarly on protein folding stability
Author(s) -
Zhou Huan-Xiang
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.01.030
Subject(s) - chemistry , macromolecular crowding , polymer , protein folding , folding (dsp implementation) , thermodynamics , protein stability , macromolecule , chemical physics , physics , organic chemistry , biochemistry , electrical engineering , engineering
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.