Department of Chemistry, The University of Texas at El Paso, 500 W. University Ave, El Paso, TX, USA, 79968.
Adv Exp Med Biol. 2017;966:163-179. doi: 10.1007/5584_2017_88.
The folding of disulfide bond containing proteins proceeds in a biphasic manner. Initially, cysteines are oxidized to form disulfide bonds. Structure is largely absent during this phase. Next, when a minimally correct number of native linkages of disulfide bonds have been acquired, the biopolymer conformationally folds into the native, or a native-like, state. Thus, at the end of this "oxidative folding" process, a stable and biologically active protein is formed. This review focuses on dissecting the "structure-forming step" in oxidative protein folding. The ability to follow this pivotal step in protein maturation in somewhat detail is uniquely facilitated in "oxidative" folding scenarios. We review this step using bovine pancreatic Ribonuclease A as a model while recognizing the impact that this step has in subcellular trafficking and protein aggregation.
含二硫键的蛋白质的折叠过程呈两相方式进行。最初，半胱氨酸被氧化形成二硫键。在此阶段，结构基本不存在。接下来，当获得最小数量的正确的天然二硫键连接时，生物聚合物构象折叠成天然或类似天然的状态。因此，在这个“氧化折叠”过程结束时，形成稳定的、具有生物活性的蛋白质。这篇综述重点剖析了氧化蛋白折叠中的“形成结构的步骤”。在“氧化”折叠情况下，能够详细跟踪蛋白质成熟过程中的这个关键步骤的能力是独一无二的。我们使用牛胰核糖核酸酶 A 作为模型来回顾这一步骤，同时认识到这一步骤对细胞内运输和蛋白质聚集的影响。
