Protein conformational changes and protonation dynamics probed by a single shot using quantum-cascade-laser-based IR spectroscopy.

Autor: Schubert, Luiz, Langner, Pit, Ehrenberg, David, Lorenz-Fonfria, Victor A., Heberle, Joachim
Předmět:
Zdroj: Journal of Chemical Physics; 5/28/2022, Vol. 156 Issue 20, p1-9, 9p
Abstrakt: 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. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index