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The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coli.
The urea-induced equilibrium unfolding of the alpha subunit of tryptophan synthase (alphaTS), a single domain alpha/beta barrel protein, displays a stable intermediate at approximately 3.2 M urea when monitored by absorbance and circular dichroism (CD) spectroscopy (Matthews CR, Crisanti MM, 1981, B...
Sparad:
| Huvudupphovsmän: | , , |
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| Materialtyp: | Artigo |
| Språk: | Inglês |
| Publicerad: |
Cold Spring Harbor Laboratory Press
1999
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| Ämnen: | |
| Länkar: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2144415/ https://ncbi.nlm.nih.gov/pubmed/10452606 |
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