2026-04-29T04:08:32Zhttps://repisalud.isciii.es/rest/oai/requestoai:repisalud.isciii.es:20.500.12105/83072024-09-27T09:31:51Zcom_20.500.12105_19604com_20.500.12105_2051col_20.500.12105_19605
Repisalud
author
Pimenta-Lopes, Carolina
author
Suay-Corredera, Carmen
author
Velazquez-Carreras, Diana
author
Sanchez-Ortiz, David
author
Alegre-Cebollada, Jorge
funder
Ministerio de Ciencia, Innovación y Universidades (España)
funder
Comunidad de Madrid (España)
funder
Centro Nacional de Investigaciones Cardiovasculares Carlos III (España)
funder
Instituto de Salud Carlos III
funder
Fundación ProCNIC
2019-08-21T07:17:05Z
2019-08-21T07:17:05Z
2019-08
Comms Phys. 2019; 2(1):91
2399-3650
http://hdl.handle.net/20.500.12105/8307
10.1038/s42005-019-0192-y
Communications Physics
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.
eng
Concurrent atomic force spectroscopy
journal article
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URL
https://repisalud.isciii.es/bitstreams/29e2ce96-5181-4b9d-a341-9166ab148318/download
File
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application/pdf
ConcurrentAtomicForceSpectroscopy_2019.pdf
URL
https://repisalud.isciii.es/bitstreams/161d439e-a2a7-4092-991b-95c5923c7d31/download
File
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text/plain
ConcurrentAtomicForceSpectroscopy_2019.pdf.txt