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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...

Deskribapen osoa

Gorde:
Xehetasun bibliografikoak
Egile Nagusiak: Louzada, Paulo Roberto, Sebollela, Adriano, Scaramello, Marcelo E., Ferreira, Sérgio T.
Formatua: Artigo
Hizkuntza:Inglês
Argitaratua: Biophysical Society 2003
Gaiak:
Sarrera elektronikoa:https://ncbi.nlm.nih.gov/pmc/articles/PMC1303601/
https://ncbi.nlm.nih.gov/pubmed/14581225
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