Unfolding pathways of human serum albumin: Evidence for sequential unfolding and folding of its three domains

被引：61

作者：

Santra, MK ^{[1
]}

Banerjee, A ^{[1
]}

Rahaman, O ^{[1
]}

Panda, D ^{[1
]}

机构：

[1] Indian Inst Technol, Sch Biosci & Bioengn, Bombay 400076, Maharashtra, India

来源：

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 2005年 / 37卷 / 04期

关键词：

HSA; pyrene maleimide; NPA; GdnHCl; sequential unfolding;

D O I：

10.1016/j.ijbiomac.2005.10.009

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Human serum albumin (HSA) contains three alpha-helical domains The unfolding process of these domains was monitored using covalently bound fluorescence probes; domain I was monitored by N-(1-pyrene)maleimide (PM) conjugated with cys-34, domain II was monitored by the lone tryptophan residue and domain III was followed by p-nitrophenyl anthranilate (NPA) conjugated with Tyrosine-411 (Tyr-411). Using domain-specific probes, we found that guanidium hydrochloride-induced unfolding of HSA occurred sequentially. The unfolding of domain II preceded that of domain I and the unfolding of domain III followed that of domain I. In addition, the domains I and III refolded within the dead time of the fluorescence recovery experiment while the refolding of domain II occurred slowly. The results suggest that individual domain of a multi-domain protein can fold and unfold sequentially. (c) 2005 Elsevier B.V. All rights reserved.

引用

页码：200 / 204

页数：5