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Length of polyglutamine tract affects secondary and tertiary structures of huntingtin protein.

Abstract：

:The role of polyglutamine (polyQ) tract on protein stability and disease pathology remains ambiguous. We monitored the unfolding/refolding patterns of huntingtin proteins with varying polyQ lengths. In the presence of urea, minor differences in unfolding and refolding efficiencies were observed. However, in the presence of guanidinium hydrochloride, the protein with a longer polyQ stretch was able to regain its secondary but not tertiary structure on step-wise removal of denaturant. Thus, in case of Huntington's disease, the higher aggregation propensity of the mutant protein is likely to be due to the lower stability of the protein due to elongated polyQ tract.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Vachharajani SN,Chaudhary RK,Prasad S,Roy I

doi

10.1016/j.ijbiomac.2012.07.022

subject

Has Abstract

pub_date

2012-12-01 00:00:00

pages

920-5

issue

5

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(12)00295-4

journal_volume

51

pub_type

杂志文章

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