Stabilization of proteins in confined spaces
Stabilization of proteins in confined spaces
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DOI：
10.1021/bi0155504
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发表时间：
2001-09-25
期刊：
影响因子：
2.9
通讯作者：
Dill, KA
中科院分区：
文献类型：
--
作者：
Zhou, HX;Dill, KA
我们提出的理论表明，将蛋白质限制在一个小的惰性空间（“笼子”）中应该可以稳定蛋白质，防止其可逆展开。此类空间的例子可能包括色谱柱内的孔、伴侣蛋白中的安芬森笼、核糖体的内部或细胞内的空间闭塞区域。限制消除了展开链的一些扩展构型，将平衡从展开状态转向自然状态。当溶剂从天然条件变为变性条件时，预计有限空间中蛋白质的分配系数将显着降低。小笼预计可将天然状态的稳定性提高多达 15 kcal/mol。限制也可能增加蛋白质或 RNA 折叠的速率。
We present theory showing that confining a protein to a small inert space (a "cage") should stabilize the protein against reversible unfolding. Examples of such spaces might include the pores within chromatography columns, the Anfinsen cage in chaperonins, the interiors of ribosomes, or regions of steric occlusion inside cells. Confinement eliminates some expanded configurations of the unfolded chain, shifting the equilibrium from the unfolded state toward the native state. The partition coefficient for a protein in a confined space is predicted to decrease significantly when the solvent is changed from native to denaturing conditions. Small cages are predicted to increase the stability of the native state by as much as 15 kcal/mol. Confinement may also increase the rates of protein or RNA folding.