Molecular chaperones in protein folding: the art of avoiding sticky situations

Hartl, F. U.; Hlodan, R.; Langer, T.

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

Molecular chaperones in protein folding: the art of avoiding sticky situations

MPS-Authors

/persons/resource/persons278030

Langer, T.
Department Langer - Mitochondrial Proteostasis, Max Planck Institute for Biology of Ageing, Max Planck Society;

External Resource

https://www.ncbi.nlm.nih.gov/pubmed/7908149
(Any fulltext)

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Hartl, F. U., Hlodan, R., & Langer, T. (1994). Molecular chaperones in protein folding: the art of avoiding sticky situations. Trends Biochem Sci, 19(1), 20-5.

Cite as: https://hdl.handle.net/21.11116/0000-000B-6FCA-6

Abstract

Molecular chaperones are a class of proteins that interact with the non-native conformations of other proteins. The major role of chaperones of the Hsp70 and Hsp60 families is to prevent aggregation of newly synthesized polypeptides and then to mediate their folding to the native state. As a result of functional studies of these proteins, there has been a revision of the long-held view that protein folding in the cell is a spontaneous process.