Single molecule secondary structure determination of proteins through infrared absorption nanospectroscopy

Francesco Simone Ruggeri (), Benedetta Mannini, Roman Schmid, Michele Vendruscolo and Tuomas P. J. Knowles ()
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Francesco Simone Ruggeri: University of Cambridge
Benedetta Mannini: University of Cambridge
Roman Schmid: University of Cambridge
Michele Vendruscolo: University of Cambridge
Tuomas P. J. Knowles: University of Cambridge

Nature Communications, 2020, vol. 11, issue 1, 1-9

Abstract: Abstract The chemical and structural properties of biomolecules determine their interactions, and thus their functions, in a wide variety of biochemical processes. Innovative imaging methods have been developed to characterise biomolecular structures down to the angstrom level. However, acquiring vibrational absorption spectra at the single molecule level, a benchmark for bulk sample characterization, has remained elusive. Here, we introduce off-resonance, low power and short pulse infrared nanospectroscopy (ORS-nanoIR) to allow the acquisition of infrared absorption spectra and chemical maps at the single molecule level, at high throughput on a second timescale and with a high signal-to-noise ratio (~10–20). This high sensitivity enables the accurate determination of the secondary structure of single protein molecules with over a million-fold lower mass than conventional bulk vibrational spectroscopy. These results pave the way to probe directly the chemical and structural properties of individual biomolecules, as well as their interactions, in a broad range of chemical and biological systems.

Date: 2020
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DOI: 10.1038/s41467-020-16728-1

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