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Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein

Nature Structural Biology volume 3, pages 868–873 (1996)Cite this article

Abstract

It is generally assumed that folding intermediates contain partially formed native-like secondary structures. However, if we consider the fact that the conformational stability of the intermediate state is simpler than that of the native state, it would be expected that the secondary structures in a folding intermediate would not necessarily be similar to those of the native state. β-Lactoglobulin is a predominantly β-sheet protein, although it has a markedly high intrinsic preference for α-helical structure. We have studied the refolding kinetics of bovine β-lactoglobulin using stopped-flow circular dichroism and find that a partly α-helical intermediate accumulates transiently before formation of the native β-sheets. The present results suggest that the folding reaction of β-lactoglobulin follows a non-hierarchical mechanism, in which non-native α-helical structures play important roles.

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Authors and Affiliations

  1. Department of Biology, Graduate School of Science, Osaka University, Toyonaka, Osaka, 560, Japan

    Daizo Hamada & Yuji Goto

  2. Department of Physics, School of Science, Kwansei Gakuin University, Nishinomiya, Hyogo, 662, Japan

    Shin-ichi Segawa

Authors
  1. Daizo Hamada
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  2. Shin-ichi Segawa
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  3. Yuji Goto
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Hamada, D., Segawa, Si. & Goto, Y. Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein. Nat Struct Mol Biol 3, 868–873 (1996). https://doi.org/10.1038/nsb1096-868

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