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Multiple Molecules of Hsc70 and a Dimer of DjA1 Independently Bind to an Unfolded Protein
Protein folding is a prominent chaperone function of the Hsp70 system. Refolding of an unfolded protein is efficiently mediated by the Hsc70 system with either type 1 DnaJ protein, DjA1 or DjA2, and a nucleotide exchange factor. A surface plasmon resonance technique was applied to investigate substr...
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| Autors principals: | , |
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| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
American Society for Biochemistry and Molecular Biology
2010
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| Matèries: | |
| Accés en línia: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2878007/ https://ncbi.nlm.nih.gov/pubmed/20363747 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M110.101501 |
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