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oai:repisalud.isciii.es:20.500.12105/83072024-09-27T09:31:51Zcom_20.500.12105_19604com_20.500.12105_2051col_20.500.12105_19605

00925njm 22002777a 4500 dc Pimenta-Lopes, Carolina author Suay-Corredera, Carmen author Velazquez-Carreras, Diana author Sanchez-Ortiz, David author Alegre-Cebollada, Jorge author 2019-08 Force-spectroscopy by atomic force microscopy (AFM) is the technique of choice to measure mechanical properties of molecules, cells, tissues and materials at the nano and micro scales. However, unavoidable calibration errors of AFM probes make it cumbersome to quantify modulation of mechanics. Here, we show that concurrent AFM force measurements enable relative mechanical characterization with an accuracy that is independent of calibration uncertainty, even when averaging data from multiple, independent experiments. Compared to traditional AFM, we estimate that concurrent strategies can measure differences in protein mechanical unfolding forces with a 6-fold improvement in accuracy or a 30-fold increase in throughput. Prompted by our results, we demonstrate widely applicable orthogonal fingerprinting strategies for concurrent single-molecule nanomechanical profiling of proteins. Comms Phys. 2019; 2(1):91 2399-3650 http://hdl.handle.net/20.500.12105/8307 10.1038/s42005-019-0192-y Communications Physics Concurrent atomic force spectroscopy