Effect of non-native helix destabilization on the folding of equine β-lactoglobulin.

Abstract:

:β-lactoglobulin forms a non-native α-helix during an early stage of folding. To address the role of the non-native structure in the folding process, we designed several mutants of equine β-lactoglobulin with reduced helical propensity in the non-native helix region. One of them, A123T, showed a similar structure to that of the wild-type protein; its folding kinetics was investigated by stopped-flow circular dichroism (CD) and fluorescence. Although A123T showed a reduced burst-phase CD intensity, its folding rate was similar to that of the wild-type protein, which indicated that the formation of the non-native helix does not accelerate or decelerate the folding reaction.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Okabe T,Miyajima T,Nakagawa K,Tsukamoto S,Fujiwara K,Ikeguchi M

doi

10.1093/jb/mvu043

subject

Has Abstract

pub_date

2014-11-01 00:00:00

pages

291-7

issue

5

eissn

0021-924X

issn

1756-2651

pii

mvu043

journal_volume

156

pub_type

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