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2000
Volume 11, Issue 2
  • ISSN: 0929-8665
  • E-ISSN: 1875-5305

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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/content/journals/ppl/10.2174/0929866043478257
2004-04-01
2025-10-13
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  • Article Type:
    Review Article
Keyword(s): molten globule state; trypsin; urea denaturation
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