Journal
JOURNAL OF CHEMICAL PHYSICS
Volume 156, Issue 20, Pages -Publisher
AIP Publishing
DOI: 10.1063/5.0088526
Keywords
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Funding
- Raphael Horvath and Markus Mangold (IRsweep, Staefa, Switzerland)
- International Max Planck Research School (IMPRS) on Multiscale Bio-Systems
- Ministerio de Ciencia e Innovacion (MICINN)-Agencia Estatal de Investigacion (AEI) [PID2019-106103GB-I00]
- German Research Foundation [EXC 2008/1 (UniSysCat), 390540038]
- SFB [1078]
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Mid-IR spectroscopy is used to investigate protein reactions. In this study, quantum-cascade-laser-based dual-comb spectroscopy is used to probe protein conformational changes and protonation events by a single-shot experiment. The feasibility of QCL-based infrared spectroscopy in monitoring irreversible reactions is demonstrated.
Mid-IR spectroscopy is a powerful and label-free technique to investigate protein reactions. In this study, we use quantum-cascade-laser-based dual-comb spectroscopy to probe protein conformational changes and protonation events by a single-shot experiment. By using a well-characterized membrane protein, bacteriorhodopsin, we provide a comparison between dual-comb spectroscopy and our homebuilt tunable quantum cascade laser (QCL)-based scanning spectrometer as tools to monitor irreversible reactions with high time resolution. In conclusion, QCL-based infrared spectroscopy is demonstrated to be feasible for tracing functionally relevant protein structural changes and proton translocations by single-shot experiments. Thus, we envisage a bright future for applications of this technology for monitoring the kinetics of irreversible reactions as in (bio-)chemical transformations. (C) 2022 Author(s).
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