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

Takahiro Okabe | Zendy; Toshiaki Miyajima | Zendy; Kanako Nakagawa | Zendy; Seiichi Tsukamoto | Zendy; Kazuo Fujiwara | Zendy; Masamichi Ikeguchi | Zendy

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

Author(s) -

Takahiro Okabe,

Toshiaki Miyajima,

Kanako Nakagawa,

Seiichi Tsukamoto,

Kazuo Fujiwara,

Masamichi Ikeguchi

Publication year - 2014

Publication title -

the journal of biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.28

H-Index - 115

eISSN - 1756-2651

pISSN - 0021-924X

DOI - 10.1093/jb/mvu043

Subject(s) - folding (dsp implementation) , circular dichroism , chemistry , protein folding , helix (gastropod) , biophysics , crystallography , kinetics , fluorescence , biochemistry , biology , physics , ecology , quantum mechanics , snail , electrical engineering , engineering

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.

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