Principles of chaperone-mediated protein folding Journal Article
| Author: | Hartl, F. U. |
| Article Title: | Principles of chaperone-mediated protein folding |
| Abstract: | The recent discovery of molecular chaperones and their functions has changed dramatically our view of the processes underlying the folding of proteins in vivo. Rather than folding spontaneously, most newly synthesized polypeptide chains seem to acquire their native conformations in a reaction mediated by chaperone proteins. Different classes of molecular chaperones, such as the members of the Hsp70 and Hsp60 families of heat-shock proteins, cooperate in a coordinated pathway of cellular protein folding. |
| Keywords: | protein conformation; chemistry; heat shock protein 70; protein folding; hsp70 heat-shock proteins; chaperone; molecular chaperones; chaperonin 60; article; chaperonin |
| Journal Title: | Philosophical Transactions of the Royal Society B: Biological Sciences |
| Volume: | 348 |
| Issue: | 1323 |
| ISSN: | 0962-8436 |
| Publisher: | Royal Society |
| Date Published: | 1995-04-29 |
| Start Page: | 107 |
| End Page: | 112 |
| Language: | English |
| DOI: | 10.1098/rstb.1995.0051 |
| PUBMED: | 7770479 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Article -- Export Date: 28 August 2018 -- Source: Scopus |
