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2000
Volume 10, Issue 1
  • ISSN: 0929-8665
  • E-ISSN: 1875-5305

Abstract

Temperature and Guanidine hydrochloride induced unfolding transitions of papain at pH 2.0 are biphasic implying independent and sequential unfolding of its two domains. To determine the order of unfolding, the active site located in the interface of the domains was labeled with an environment specific fluorescent probe (1,8-IAEDANS). Unfolding of this complex relative to the free protein followed by intrinsic and extrinsic fluorescence measurements suggests that the N domain unfolds initially in the sequential unfolding of domains

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/content/journals/ppl/10.2174/0929866033408327
2003-02-01
2025-05-07
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/content/journals/ppl/10.2174/0929866033408327
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  • Article Type:
    Review Article
Keyword(s): domain; guhcl; iaedans; molten globule; order of sequential unfolding; papain; temperature
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