| Literature DB >> 12618784 |
Ingo Schwaiger1, Clara Sattler, Daniel R Hostetter, Matthias Rief.
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 elasticity to synaptic fusion. Beyond their importance in biology, coiled-coils have also attracted interest as programmable protein sequences for the design of novel hydrogels and materials. 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.Entities:
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Year: 2002 PMID: 12618784 DOI: 10.1038/nmat776
Source DB: PubMed Journal: Nat Mater ISSN: 1476-1122 Impact factor: 43.841