Urea-Induced Denaturation of β-Trypsin: An Evidence for a Molten Globule State

Author(s): Maria Helena Nasser Brumano, Maria Goreti de Almeida Oliveira.

Journal Name: Protein & Peptide Letters

Volume 11 , Issue 2 , 2004

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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.

Keywords: trypsin, urea denaturation,, molten globule state.

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Article Details

Year: 2004
Page: [133 - 140]
Pages: 8
DOI: 10.2174/0929866043478257
Price: $58

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