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

Abstract：

:Human serum albumin (HSA) contains three alpha-helical domains (I-III). 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.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Santra MK,Banerjee A,Rahaman O,Panda D

doi

10.1016/j.ijbiomac.2005.10.009

keywords:

subject

Has Abstract

pub_date

2005-12-15 00:00:00

pages

200-4

issue

4

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(05)00234-5

journal_volume

37

pub_type

杂志文章

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