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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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Bibliografski detalji
Glavni autori: Zahn, Ralph, Buckle, Ashley M., Perrett, Sarah, Johnson, Christopher M., Corrales, Fernando J., Golbik, Ralph, Fersht, Alan R.
Format: Artigo
Jezik:Inglês
Izdano: The National Academy of Sciences of the USA 1996
Teme:
Online pristup:https://ncbi.nlm.nih.gov/pmc/articles/PMC26349/
https://ncbi.nlm.nih.gov/pubmed/8986757
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