- Title
- General structural and functional features of molecular chaperones:
- Creator
- Edkins, Adrienne L
- Creator
- Boshoff, Aileen
- Date Issued
- 2014
- Date
- 2014
- Type
- text
- Type
- book
- Identifier
- http://hdl.handle.net/10962/164808
- Identifier
- vital:41174
- Identifier
- ISBN 978-94-007-7437-7
- Identifier
- DOI: 10.1007/978-94-007-7438-4_2
- Description
- Molecular chaperones are a group of structurally diverse and highly conserved ubiquitous proteins. They play crucial roles in facilitating the correct folding of proteins in vivo by preventing protein aggregation or facilitating the appropriate folding and assembly of proteins. Heat shock proteins form the major class of molecular chaperones that are responsible for protein folding events in the cell. This is achieved by ATP-dependent (folding machines) or ATP-independent mechanisms (holders). Heat shock proteins are induced by a variety of stresses, besides heat shock. The large and varied heat shock protein class is categorised into several subfamilies based on their sizes in kDa namely, small Hsps (HSPB), Hsp40 (DNAJ), Hsp60 (HSPD/E; Chaperonins), Hsp70 (HSPA), Hsp90 (HSPC), and Hsp100.
- Format
- 41 pages
- Format
- Publisher
- Springer
- Language
- English
- Relation
- Edkins, A.L. and Boshoff, A., 2014. General structural and functional features of molecular chaperones. In Heat Shock Proteins of Malaria (pp. 5-45). Springer, Dordrecht
- Rights
- Publisher
- Rights
- Use of this resource is governed by the terms and conditions of the SpringerLink Terms of Use Statement ( https://link.springer.com/termsandconditions)
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RU DST/NRF SARChI for Molecular and Cellular Biology of the Eukaryotic Stress Response
Boshoff, Aileen (Assoc Prof)
RU Department of Biochemistry, Microbiology and Biotechnology
Edkins, Adrienne Lesley (Associate Prof)
RU Books and Book Chapters
SDG 03. Good Health and Well-Being
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