Abstract
Time-resolved Fourier transform infrared spectroscopy (FT-IR) has been proven to be an excellent method with important applications in bioscience. In particular, it is possible to monitor the temporal evolution of the reaction mechanism of complex machineries as membrane proteins, where other techniques encounter significant experimental difficulties. Here, we summarize the classical principles and experimental realizations of time-resolved FT-IR spectroscopy together with new developments realized in our laboratory. Examples from applications to retinal proteins are reviewed that showcase the impact of time-resolved FT-IR spectroscopy on the understanding of protein reactions on the level of single bonds.
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