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Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions
Published on: April 4, 2014
Urea-induced denaturation of beta-trypsin: an evidence for a molten globule state
Maria Helena Nasser Brumano1, Maria Goreti de Almeida Oliveira
1Departamento de Bioquimica e Biologia Molecular, Universidade Federal de Vicosa, Vicosa, MG, 36571-000, Brazil.
Abstract:
The denaturation of beta-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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