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Chaperone activity and structure of monomeric polypeptide binding domains of GroEL
The chaperonin GroEL is a large complex composed of 14 identical 57-kDa subunits that requires ATP and GroES for some of its activities. We find that a monomeric polypeptide corresponding to residues 191 to 345 has the activity of the tetradecamer both in facilitating the refolding of rhodanese and...
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| Main Authors: | , , , , , , |
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| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
The National Academy of Sciences of the USA
1996
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC26349/ https://ncbi.nlm.nih.gov/pubmed/8986757 |
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