Abstract
Publisher Summary This chapter discusses the folding of soluble globular proteins as assisted by proteins called “chaperonins,” which can operate in vivo and in vitro , and “amphiphiles” such as detergents that appear to share some mechanistic similarities with the chaperonins and provide both basic and practical understanding of folding assistance. The chapter focuses on the folding of proteins for which aggregation and/or association are major side paths that compete with folding. The chapter discusses studies of the enzyme rhodanese (EC 2.8.1.1), the usefulness of rhodanese as a folding model, and issues related to chaperonin-assisted folding. Cellular proteins such as protein disulfide isomerase and prolyl isomerase have been identified as catalysts of processes that can influence the folding of proteins. The sequence of a native protein spontaneously adopts the narrow distribution of conformational states associated with the originally folded protein.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
