Chaperonins keeping a lid on folding proteins
| dc.contributor.author | Kusmierczyk, Andrew R | |
| dc.contributor.author | Martin, Jörg | |
| dc.date.accessioned | 2014-10-07T15:50:19Z | |
| dc.date.available | 2014-10-07T15:50:19Z | |
| dc.date.issued | 2001-09 | |
| dc.description.abstract | Two classes of chaperonins are known in all groups of organisms to participate in the folding of newly synthesized proteins. Whereas bacterial type I chaperonins use a reversibly binding cofactor to temporarily sequester folding substrate proteins within the cylindrical chaperonin cavity, type II chaperonins in archaea and the eukaryotic cytosol appear to have evolved a built-in lid for this purpose. Not entirely surprisingly, this has consequences for the folding modes of the two types of chaperonins. | en_US |
| dc.identifier.citation | Kusmierczyk, A. R., & Martin, J. (2001). Chaperonins–keeping a lid on folding proteins. FEBS letters, 505(3), 343-347. | en_US |
| dc.identifier.uri | https://hdl.handle.net/1805/5205 | |
| dc.language.iso | en_US | en_US |
| dc.subject | protein folding | en_US |
| dc.subject | chaperonins | en_US |
| dc.subject | groEL | en_US |
| dc.title | Chaperonins keeping a lid on folding proteins | en_US |
| dc.type | Article | en_US |