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Electrostatic interactions affecting the active site of class sigma glutathione S-transferase.

We have shown previously that the solvent-induced equilibrium unfolding mechanism of class Sigma glutathione S-transferase (GST) is strongly affected by ionic strength [Stevens, Hornby, Armstrong and Dirr (1998) Biochemistry 37, 15534-15541]. The protein is dimeric and has a hydrophilic subunit inte...

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Main Authors: Stevens, J M, Armstrong, R N, Dirr, H W
Formato: Artigo
Idioma:Inglês
Publicado: 2000
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Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC1220947/
https://ncbi.nlm.nih.gov/pubmed/10727418
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