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Bipartite structure of the α-lactalbumin molten globule

Nature Structural Biology volume 2, pages 281–286 (1995)Cite this article

Abstract

Molten globules are thought to be general intermediates in protein folding. Apparently conflicting studies have failed to clarify whether one of the best characterized molten globules, that of α-lactalbumin, resembles an expanded native-like protein or a nonspecific collapsed polypeptide. Here we show that the molten globule properties of α-lactalbumin are largely confined to one of its two domains. The α-helical domain forms a helical structure with a native-like tertiary fold, while the β-sheet domain is largely unstructured. Molten globules thus possess a native-like backbone topology, but this topology does not necessarily encompass the entire polypeptide chain. Our studies indicate that molten globules provide an approximate solution to, and considerable simplification of the protein folding problem.

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Authors and Affiliations

  1. Howard Hughes Medical Institute, Whitehead Institute for Biomedical Research, Department of Biology, Massachusetts Institute of Technology, Nine Cambridge Center, Cambridge, Massachusetts, 02142, USA

    Lawren C. Wu, Zheng-yu Peng & Peter S. Kim

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  1. Lawren C. Wu
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  2. Zheng-yu Peng
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  3. Peter S. Kim
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Wu, L., Peng, Zy. & Kim, P. Bipartite structure of the α-lactalbumin molten globule. Nat Struct Mol Biol 2, 281–286 (1995). https://doi.org/10.1038/nsb0495-281

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