Uverskiĭ V N, Semisotnov G V, Ptitsyn O B
Biofizika. 1993 Jan-Feb;38(1):37-46.
The equilibrium Gu-HCl-induced denaturation of bovine carbonic anhydrase B and beta-lactamase from Staphylococcus aureus was studied at 4 degrees C by the multiparametric approach. With the use of fast protein size-exclusion chromatography (FPLC) it has been shown that in the region of the molten globule-random coil transition the distribution function of the protein molecules on size is bimodal, i.e. the protein molecules (which are already denatured) can only in one of two conformational states. Consequently the unfolding of the molten globule can be of "all-or-none" character. This means that a protein molecule can be at least in three discrete states: the native, the molten globule and unfolded.
在4℃下，采用多参数方法研究了胍盐酸盐诱导的牛碳酸酐酶B和金黄色葡萄球菌β-内酰胺酶的平衡变性。通过快速蛋白质尺寸排阻色谱法（FPLC）表明，在熔球态-无规卷曲转变区域，蛋白质分子按大小的分布函数是双峰的，即已变性的蛋白质分子只能处于两种构象状态之一。因此，熔球态的去折叠可能具有“全或无”的特征。这意味着蛋白质分子至少可以处于三种离散状态：天然态、熔球态和去折叠态。
