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Do Chaperonins Boost Protein Yields by Accelerating Folding or Preventing Aggregation?
The GroEL chaperonin has the ability to behave as an unfoldase, repeatedly denaturing proteins upon binding, which in turn can free them from kinetic traps and increase their folding rates. The complex formed by GroEL+GroES+ATP can also act as an infinite dilution cage, enclosing proteins within a p...
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| Hlavní autoři: | , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
The Biophysical Society
2008
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2275679/ https://ncbi.nlm.nih.gov/pubmed/18192377 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1529/biophysj.107.113209 |
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