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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.
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
Affiliation:
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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Cite this article as:
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
DOI https://dx.doi.org/10.2174/0929866043478257 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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