Please use this identifier to cite or link to this item:http://hdl.handle.net/20.500.12105/8307
Concurrent atomic force spectroscopy
Pimenta-Lopes, Carolina CNIC | Suay-Corredera, Carmen CNIC | Velazquez-Carreras, Diana CNIC | Sanchez-Ortiz, David CNIC | Alegre-Cebollada, Jorge CNIC
Comms Phys. 2019; 2(1):91
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.
Files in this item
- ConcurrentAtomicForceSpectrosc ...