二硫键在稳定蛋白质构象和保持蛋白质活性方面起重要作用，但是天然二硫键的形成是许多蛋白正确折叠中的限速步骤。随着对二硫键异构酶和折叠中间体研究的深入，富含二硫键蛋白的折叠机制逐渐为人们所认识。在本文中，着重从体内二硫键的形成和体外蛋白质的氧化折叠两个方面对二硫键蛋白的折叠机制及其在基因工程中的实践应用等做一综述，对深入研究提高富含二硫键的重组活性蛋白质的产率起重要指导意义。
Abstract: Disulfide bonds play an important role in stability of protein conformation and maintaining of protein activity. However, formation of natural disulfide bonds is a rate-limiting step in protein correct folding. With study on protein disulfide isomerase and folding intermediates, folding mechanism of disulfide-rich proteins has been clarified gradually. The protein folding mechanism is focused on in this review, which was understood by formation of disulfide bonds in vivo and protein oxidative folding in vitro, and its application in genetic engineering. These new findings may represent future directions for improving the quality of recombinant protein which is rich with disulfide bonds
许成钢,范晓军,付月君,梁爱华. 二硫键的形成与蛋白质的氧化折叠[J]. 中国生物工程杂志, 2008, 28(专刊): 259-264.
Cheng-Gang Xu Xiao-Jun FAN Yue-Jun FU Ai-Hua Liang. Formation of disulfide bonds and protein oxidative folding. China Biotechnology, 2008, 28(专刊): 259-264.
https://manu60.magtech.com.cn/biotech/CN/ 或 https://manu60.magtech.com.cn/biotech/CN/Y2008/V28/I专刊/259
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