Intermolecular aggregations are responsible for the slow kinetics observed in the folding of cytochrome c at neutral pH.
Intermolecular aggregations are responsible for the slow kinetics observed in the folding of cytochrome c at neutral pH.
复制标题
分子间聚集是造成细胞色素 c 在中性 pH 条件下折叠动力学缓慢的原因。
DOI：
10.1006/jmbi.1999.3226
复制
发表时间：
1999
影响因子：
5.6
通讯作者：
Bai,Y
中科院分区：
文献类型：
--
作者：
Nawrocki,JP;Chu,RA;Pannell,LK;Bai,Y
马细胞色素c在低蛋白浓度（26 μM）下的折叠消除了之前在pH 6.2和10 °C下氢交换脉冲标记实验中观察到的缓慢动力学阶段（时间常数为3秒）。结果表明，这种缓慢的折叠阶段是由分子间聚集引起的。由于非均相动力学是一个非常普遍的特征，其特征在于脉冲氢交换耦合二维NMR的蛋白质折叠，我们的实验结果表明，聚集体也可能是负责其他蛋白质的复杂折叠动力学。这是可能的，因为这些实验是在相对高的蛋白质浓度下进行的。
Folding of equine cytochrome c at a low protein concentration (26 μM) eliminated a slow kinetic phase (time constant three seconds) that was observed in the previous hydrogen exchange pulse-labeling experiments at pH 6.2 and 10 °C. It was demonstrated that this slow folding phase was caused by intermolecular aggregations. Because heterogeneous kinetics is a very general feature in the folding of proteins characterized by pulsed hydrogen exchange coupled with two-dimensional NMR, our experimental results suggest aggregations might also be responsible for the complex folding kinetics of other proteins. This is possible since these experiments were performed at relatively high protein concentrations.