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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Detalhes bibliográficos

Publicado no:	Proc Natl Acad Sci U S A
Principais autores:	Zahn, Ralph, Buckle, Ashley M., Perrett, Sarah, Johnson, Christopher M., Corrales, Fernando J., Golbik, Ralph, Fersht, Alan R.
Formato:	Artigo
Idioma:	Inglês
Publicado em:	National Academy of Sciences 1996
Assuntos:	Biological Sciences
Acesso em linha:	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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