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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...

詳細記述

保存先:
書誌詳細
主要な著者: van Mierlo, C. P., van Dongen, W. M., Vergeldt, F., van Berkel, W. J., Steensma, E.
フォーマット: Artigo
言語:Inglês
出版事項: Cold Spring Harbor Laboratory Press 1998
主題:
オンライン・アクセス:https://ncbi.nlm.nih.gov/pmc/articles/PMC2143863/
https://ncbi.nlm.nih.gov/pubmed/9827999
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