The myosin coiled-coil is a truly elastic protein structure

Ingo Schwaiger; Clara Sattler; Daniel R. Hostetter; Matthias Rief

doi:10.1038/nmat776

The myosin coiled-coil is a truly elastic protein structure

Ingo Schwaiger, Clara Sattler, Daniel R. Hostetter, Matthias Rief

Research output: Contribution to journal › Article › peer-review

207 Scopus citations

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.

Original language	English
Pages (from-to)	232-235
Number of pages	4
Journal	Nature Materials
Volume	1
Issue number	4
DOIs	https://doi.org/10.1038/nmat776
State	Published - Dec 2002
Externally published	Yes

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title = "The myosin coiled-coil is a truly elastic protein structure",

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.",

author = "Ingo Schwaiger and Clara Sattler and Hostetter, {Daniel R.} and Matthias Rief",

note = "Funding Information: We thank H. Gaub, H. Grubm{\"u}ller and J. Trinick for helpful discussions. This work was supported by an SFB413 grant of the DFG. Correspondence and requests for materials should be addressed to M.R.",

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doi = "10.1038/nmat776",

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T1 - The myosin coiled-coil is a truly elastic protein structure

AU - Schwaiger, Ingo

AU - Sattler, Clara

AU - Hostetter, Daniel R.

AU - Rief, Matthias

N1 - Funding Information: We thank H. Gaub, H. Grubmüller and J. Trinick for helpful discussions. This work was supported by an SFB413 grant of the DFG. Correspondence and requests for materials should be addressed to M.R.

PY - 2002/12

Y1 - 2002/12

N2 - 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.

AB - 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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The myosin coiled-coil is a truly elastic protein structure

Abstract

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