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Predissociated Dimers and Molten Globule Monomers in the Equilibrium Unfolding of Yeast Glutathione Reductase

The equilibrium unfolding of dimeric yeast glutathione reductase (GR) by guanidine hydrochloride (GdnHCl) was investigated. Unfolding was monitored by a variety of techniques, including intrinsic fluorescence emission, anisotropy and iodide quenching measurements, far-ultraviolet circular dichroism...

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Библиографические подробности
Главные авторы: Louzada, Paulo Roberto, Sebollela, Adriano, Scaramello, Marcelo E., Ferreira, Sérgio T.
Формат: Artigo
Язык:Inglês
Опубликовано: Biophysical Society 2003
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Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC1303601/
https://ncbi.nlm.nih.gov/pubmed/14581225
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