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...
Uloženo v:
| Vydáno v: | Proc Natl Acad Sci U S A |
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| Hlavní autoři: | , , , , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
National Academy of Sciences
1996
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC26349/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8986757/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.93.26.15024 |
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