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
Keywords: papain, molten globule, order of sequential unfolding, domain, guhcl, temperature, iaedans
Protein & Peptide Letters
Title: N-Terminal Domain Unfolds First in the Sequential Unfolding of Papain
Volume: 10 Issue: 1
Author(s): Yagya Valkya Sharma and M. V. Jagannadham.
Affiliation:
Keywords: papain, molten globule, order of sequential unfolding, domain, guhcl, temperature, iaedans
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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Cite this article as:
Sharma Valkya Yagya and Jagannadham. V. M., N-Terminal Domain Unfolds First in the Sequential Unfolding of Papain, Protein & Peptide Letters 2003; 10 (1) . https://dx.doi.org/10.2174/0929866033408327
DOI https://dx.doi.org/10.2174/0929866033408327 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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