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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...

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Detalhes bibliográficos
Main Authors: Gualfetti, P. J., Bilsel, O., Matthews, C. R.
Formato: Artigo
Idioma:Inglês
Publicado em: Cold Spring Harbor Laboratory Press 1999
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2144415/
https://ncbi.nlm.nih.gov/pubmed/10452606
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