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Temperature-favoured assembly of collagen is driven by hydrophilic not hydrophobic interactions

Nature Structural Biology volume 2, pages 205–210 (1995)Cite this article

Abstract

It has become almost axiomatic that protein folding and assembly are dominated by the hydrophobic effect. The contributions from this, and other, hydrophilic interactions can now be better distinguished by direct measurement of forces between proteins. Here we report the measurement of forces between triple helices of type I collagen at different temperatures, pH and solute concentrations. We separate repulsive and attractive components of the net force and analyze the origin of the attraction responsible for the collagen self-assembly. In this case the role of the hydrophobic effect appears to be negligible. Instead, water-mediated hydrogen bonding between polar residues is the most consistent explanation.

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Authors and Affiliations

  1. Laboratory of Structural Biology, Division of Computer Research and Technology,

    S. Leikin, D. C. Rau & V A Parsegian

  2. Division of Intramural Research, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Building 12A, Room 2041, Bethesda, Maryland, 20892, USA

    S. Leikin, D. C. Rau & V A Parsegian

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  3. V A Parsegian
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Leikin, S., Rau, D. & Parsegian, V. Temperature-favoured assembly of collagen is driven by hydrophilic not hydrophobic interactions. Nat Struct Mol Biol 2, 205–210 (1995). https://doi.org/10.1038/nsb0395-205

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