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The myosin coiled-coil is a truly elastic protein structure

Nature Materials volume 1, pages 232–235 (2002)Cite this article

Abstract

Coiled-coils occur in a variety of proteins involved in mechanical and structural tasks in the cell. Their mechanical properties are important in various contexts ranging from hair elasticity1 to synaptic fusion2. Beyond their importance in biology, coiled-coils have also attracted interest as programmable protein sequences for the design of novel hydrogels and materials3. We have studied the elastic properties of the myosin coiled-coil at the single molecule level. The coiled-coil undergoes a massive structural transition at forces between 20 and 25 pN where the coil extends to about 2.5 times its original length. Unlike all other proteins investigated mechanically so far, this transition is reversible on a timescale of less than a second, making the coiled-coil a truly elastic protein.

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Figure 1: Extensibility of the myosin coiled-coil.
Figure 2: Elasticity of the myosin coiled-coil.
Figure 3: Two-state model of coiled-coil elasticity (see Methods).

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Acknowledgements

We thank H. Gaub, H. Grubmüller and J. Trinick for helpful discussions. This work was supported by an SFB413 grant of the DFG.

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Author notes

  1. Ingo Schwaiger and Clara Sattler: These authors contributed equally to this work

Authors and Affiliations

  1. Lehrstuhl für Angewandte Physik, Amalienstrasse 54, München, 80799, Germany

    Ingo Schwaiger, Clara Sattler & Matthias Rief

  2. Department of Biochemistry B400, Stanford University School of Medicine, Stanford, 94305-5307, California, USA

    Daniel R. Hostetter

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  1. Ingo Schwaiger
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Correspondence to Matthias Rief.

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Schwaiger, I., Sattler, C., Hostetter, D. et al. The myosin coiled-coil is a truly elastic protein structure. Nature Mater 1, 232–235 (2002). https://doi.org/10.1038/nmat776

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