Department of Physics and Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306, USA.
FEBS Lett. 2013 Mar 1;587(5):394-7. doi: 10.1016/j.febslet.2013.01.030. Epub 2013 Jan 23.
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.
最近发现一种聚合物致孔剂和两种蛋白质致孔剂对糜蛋白酶抑制剂 2（CI2）的折叠稳定性有相反的影响，表明它们与 CI2 的相互作用不同。在这里，我们提出所有的大分子致孔剂都以类似的方式起作用，其中熵分量有利于折叠状态，焓分量有利于展开状态。净效应在交叉温度以下是不稳定的，但在交叉温度以上是稳定的。这一总体趋势确实在最近的实验中得到了观察，并暗示实验温度是聚合物和蛋白质致孔剂的相反拥挤效应的原因。
