The alternatively folded state of the antibody C(H)3 domain.
The alternatively folded state of the antibody C(H)3 domain.
复制标题
抗体 C(H)3 结构域的交替折叠状态。
DOI：
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发表时间：
2001
影响因子：
5.6
通讯作者：
J. Buchner
中科院分区：
文献类型：
--
作者：
M. J. Thies;R. Kammermeier;K. Richter;J. Buchner
抗体的C(H)3区域的特征是两个反平行的β-折叠形成一个二硫键连接的夹心状结构。在酸性pH值和低离子强度下，C(H)3完全展开。盐的加入将酸未折叠的蛋白质转变为交替折叠的状态，显示出特有的二级结构。从天然C(H)3到交替折叠C(H)3的转变是一个快速反应。有趣的是，该反应涉及形成由12-14个亚基组成的确定的低聚物。缔合是完全可逆的，天然二聚体在中性pH下定量重整。这种交替折叠的蛋白质对热和化学变性非常稳定，并且展开的转变是高度合作的。当t(M)为80℃时，交替折叠状态的稳定性与C(H)3的自然状态的稳定性相当。C(H)3在pH 2下确定的低聚结构似乎是合作展开转变的先决条件。
The C(H)3 domain of antibodies is characterized by two antiparallel beta-sheets forming a disulfide-linked sandwich-like structure. At acidic pH values and low ionic strength, C(H)3 becomes completely unfolded. The addition of salt transforms the acid-unfolded protein into an alternatively folded state exhibiting a characteristic secondary structure. The transition from native to alternatively folded C(H)3 is a fast reaction. Interestingly, this reaction involves the formation of a defined oligomer consisting of 12-14 subunits. Association is completely reversible and the native dimer is quantitatively reformed at neutral pH. This alternatively folded protein is remarkably stable against thermal and chemical denaturation and the unfolding transitions are highly cooperative. With a t(m) of 80 degrees C, the stability of the alternatively folded state is comparable to that of the native state of C(H)3. The defined oligomeric structure of C(H)3 at pH 2 seems to be a prerequisite for the cooperative unfolding transitions.
假单胞菌外毒素的变性样变化涉及通过 pH 和热转变表征确定的疏水性和膜渗透性。
DOI：
--
发表时间：
1990
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Jiang,JX;London,E
通讯作者：
London,E
通过远紫外停流圆二色性和 8-苯胺基-1-萘磺酸盐结合测量大肠杆菌 trp 阻压剂早期折叠中间体的结构和稳定性。
影响因子：
2.9
作者：
Mann,CJ;Matthews,CR
通讯作者：
Matthews,CR