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

Maria   Helena Nasser   Brumano; Maria   Goreti de Almeida   Oliveira

doi:10.2174/0929866043478257

Abstract

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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Protein & Peptide Letters

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

Volume: 11 Issue: 2

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

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

Abstract: 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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Brumano Helena Nasser Maria and Oliveira Goreti de Almeida Maria, Urea-Induced Denaturation of β-Trypsin: An Evidence for a Molten Globule State, Protein & Peptide Letters 2004; 11 (2) . https://dx.doi.org/10.2174/0929866043478257