Abstract
Insulin is not only a very important protein hormone in clinic but also a perfect model molecule in protein science. Almost each important achievement in the field of protein science was established from insulin study, such as protein crystal, protein sequence, protein synthesis, protein expression, and protein engineering since its discovery by Banting and Best in 1921. However, concerning in vitro folding of insulin it was not well characterized until the early 2000, probably the major difficult being that insulin consists of two polypeptide chains linked by disulfides. Because insulin is synthesized in vivo as a single chain peptide and folds well, recently the study on the in vitro folding of insulin has been investigated from single chain insulin to double chain insulin. This chapter briefly summarizes the current studies on the in vitro folding of single/double chain insulins and related proteins including their folding process, intermediates, and putative folding pathways. Besides, the common folding behavior of single/double chain insulins and related proteins and the in vivo folding process of nascent proinsulin, as suggestion or speculation, are discussed.
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Feng, YM. (2011). In Vitro Folding of Single/Double Chain Insulins and Related Proteins. In: Chang, R., Ventura, S. (eds) Folding of Disulfide Proteins. Protein Reviews, vol 14. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-7273-6_4
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DOI: https://doi.org/10.1007/978-1-4419-7273-6_4
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