期刊
PROTEIN JOURNAL
卷 40, 期 2, 页码 134-139出版社
SPRINGER
DOI: 10.1007/s10930-021-09976-7
关键词
Disulfide bonds; Oxidative protein folding; Native-like structure; Thiol-disulfide exchange reactions; Conformational folding; Protein misfolding related disorders
资金
- NIH [1SC3 GM111200 01A1]
Oxidative protein folding involves chemical and conformational folding reactions, with disulfide bonds playing a critical role. The formation of native disulfide bonds, while helpful in structure formation, must be carefully managed to avoid protein misfolding related disorders.
The folding of proteins that contain disulfide bonds is termed oxidative protein folding. It involves a chemical reaction resulting in the formation of disulfide bonds and a physical conformational folding reaction that promotes the formation of the native structure. While the presence of disulfide bonds significantly increases the complexity of the folding landscape, it is generally recognized that native disulfide bonds help funnel the trajectory towards the final folded form. Here, we review the role of disulfide bonds in oxidative protein folding and argue that even structure-inducing native disulfide bond formation treads a fine line in the regeneration of disulfide-bond-containing proteins. The translation of this observation to protein misfolding related disorders is discussed.
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