@article {36576,
	title = {Fast-folding alpha-helices as reversible strain absorbers in the muscle protein myomesin},
	journal = {Proc Natl Acad Sci U S A},
	volume = {108},
	number = {34},
	year = {2011},
	note = {Berkemeier, FelixBertz, MortenXiao, SenboPinotsis, NikosWilmanns, MatthiasGrater, FraukeRief, MatthiasengResearch Support, Non-U.S. Gov{\textquoteright}tProc Natl Acad Sci U S A. 2011 Aug 23;108(34):14139-44. doi: 10.1073/pnas.1105734108. Epub 2011 Aug 8.},
	month = {Aug 23},
	pages = {14139-44},
	edition = {2011/08/10},
	abstract = {The highly oriented filamentous protein network of muscle constantly experiences significant mechanical load during muscle operation. The dimeric protein myomesin has been identified as an important M-band component supporting the mechanical integrity of the entire sarcomere. Recent structural studies have revealed a long alpha-helical linker between the C-terminal immunoglobulin (Ig) domains My12 and My13 of myomesin. In this paper, we have used single-molecule force spectroscopy in combination with molecular dynamics simulations to characterize the mechanics of the myomesin dimer comprising immunoglobulin domains My12-My13. We find that at forces of approximately 30 pN the alpha-helical linker reversibly elongates allowing the molecule to extend by more than the folded extension of a full domain. High-resolution measurements directly reveal the equilibrium folding/unfolding kinetics of the individual helix. We show that alpha-helix unfolding mechanically protects the molecule homodimerization from dissociation at physiologically relevant forces. As fast and reversible molecular springs the myomesin alpha-helical linkers are an essential component for the structural integrity of the M band.},
	keywords = {*Protein Folding, Biomechanical Phenomena, Connectin, Kinetics, Microscopy, Atomic Force, Molecular Dynamics Simulation, Muscle Proteins/*chemistry/*metabolism, Protein Multimerization, Protein Stability, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Unfolding},
	isbn = {1091-6490 (Electronic)0027-8424 (Print)0027-8424 (Linking)},
	author = {Berkemeier, F. and Bertz, M. and S. Xiao and Pinotsis, N. and Wilmanns, M. and Grater, F. and Rief, M.}
}
