Urea-Induced Denaturation of β-Trypsin: An Evidence for a Molten Globule State
The denaturation of β-trypsin induced by urea was investigated by fluorescence and circular dichroism. A transient denatured state was found at 2 M urea in both intrinsic fluorescence spectrum and bis-(8-anilino-1-naphtalene sulfonate) (bis-ANS) binding. In addition, the absence of tertiary contacts and presence of secondary structure for this state, are consistent with an intermediate equilibrium state having features of molten globule.
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Document Type: Review Article
Affiliations: Departamento de Bioquimica e Biologia Molecular, Universidade Federal de Vicosa, Vicosa, MG, 36571-000, Brazil.
Publication date: 2004-04-01
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