The myosin coiled-coil is a truly elastic protein structure.
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.
Schwaiger
Ingo
I
Lehrstuhl für Angewandte Physik, Amalienstrasse 54, 80799 München, Germany.
Sattler
Clara
C
Hostetter
Daniel R
DR
Rief
Matthias
M
D000818:Animals; D004548:Elasticity; D018482:Muscle, Skeletal / Q000737:chemistry; D009218:Myosins / Q000737:chemistry*; D011487:Protein Conformation; D011817:Rabbits; D013816:Thermodynamics
D009218:Myosins