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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

N-Terminal Domain Unfolds First in the Sequential Unfolding of Papain

Author(s): Yagya Valkya Sharma and M. V. Jagannadham.

Volume 10, Issue 1, 2003

Page: [83 - 90] Pages: 8

DOI: 10.2174/0929866033408327

Price: $65

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


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