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The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediate.

A flavodoxin from Azotobacter vinelandii is chosen as a model system to study the folding of alpha/beta doubly wound proteins. The guanidinium hydrochloride induced unfolding of apoflavodoxin is demonstrated to be reversible. Apoflavodoxin thus can fold in the absence of the FMN cofactor. The unfold...

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Detalhes bibliográficos
Main Authors: van Mierlo, C. P., van Dongen, W. M., Vergeldt, F., van Berkel, W. J., Steensma, E.
Formato: Artigo
Idioma:Inglês
Publicado em: Cold Spring Harbor Laboratory Press 1998
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Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2143863/
https://ncbi.nlm.nih.gov/pubmed/9827999
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