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 Biochemjournal_title
Journal of biochemistryauthors
Okabe T,Miyajima T,Nakagawa K,Tsukamoto S,Fujiwara K,Ikeguchi Mdoi
10.1093/jb/mvu043subject
Has Abstractpub_date
2014-11-01 00:00:00pages
291-7issue
5eissn
0021-924Xissn
1756-2651pii
mvu043journal_volume
156pub_type
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