High-speed force spectroscopy unfolded titin at velocities reached by simulation (~4 mm/s), revealing dynamic unfolding and refolding of a β-strand pair buffering forces up to ~100 pN.
High-speed force spectroscopy enables direct comparison between experimental mechanical unfolding of titin and molecular dynamics simulations, advancing the study of biomechanical processes.
The mechanical unfolding of the muscle protein titin by atomic force microscopy was a landmark in our understanding of single-biomolecule mechanics. Molecular dynamics simulations offered atomic-level descriptions of the forced unfolding. However, experiment and simulation could not be directly compared because they differed in pulling velocity by orders of magnitude. We have developed high-speed force spectroscopy to unfold titin at velocities reached by simulation (~4 millimeters per second). We found that a small β-strand pair of an immunoglobulin domain dynamically unfolds and refolds, buffering pulling forces up to ~100 piconewtons. The distance to the unfolding transition barrier is larger than previously estimated but is in better agreement with atomistic predictions. The ability to directly compare experiment and simulation is likely to be important in studies of biomechanical processes.
Rico et al. (Thu,) conducted a other in Muscle protein titin unfolding. High-speed force spectroscopy vs. Molecular dynamics simulations was evaluated on Mechanical unfolding of titin. High-speed force spectroscopy unfolded titin at velocities reached by simulation (~4 mm/s), revealing dynamic unfolding and refolding of a β-strand pair buffering forces up to ~100 pN.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: