![]() Biomacromolecules, especially proteins with unique viscoelastic properties, primarily serve as force-sensors or conveyors and orchestrate such mechanoresponsive processes. ![]() Mechanical tension, as one of the critical cues in physiology, regulates several biological processes, including gene-expression 1, 2, 3, 4, blood-coagulation 5, cell adhesion 6, 7, muscle function 8, 9, hearing 10, 11, 12, bacterial anchorage 13, 14, 15, and more. Overall, the distinct and superior mechanical responses of cadherin-23 in handshake geometry than single protein geometry highlight a probable evolutionary drive of protein-protein complexes as force-conveyors over independent ones. Analysis of the dynamic network structure of cadherin-23 under tension indicates narrow force-distributions among residues in cadherin-23 in direct pulling, resulting in low force-dissipation paths and low resilience to force. The handshake geometry drives the force-response of cadherin-23 through different potential-energy landscapes than direct pulling. We measure higher force-resilience of cadherin-23 with preferential shorter extensions in handshake mode of pulling over the direct mode. To decipher, we choose a force-sensing protein, cadherin-23, from tip-link complex and perform SMFS using end-to-end geometry and handshake complex geometry. However, with the potential of force-steering, protein complexes possess a distinct mechano-responsive property over individual force-sensors. The physiological significance of the complex conformations in force-sensing is often disregarded as mere surge protectors. The force-responsive property of independent proteins in end-to-end geometry is studied extensively using single-molecule force spectroscopy (SMFS). ![]() Proteins commonly connect the source and response points of mechanical cues in two conformations, independent proteins in end-to-end geometry and protein complexes in handshake geometry. Proteins as force-sensors respond to mechanical cues and regulate signaling in physiology. ![]()
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