Proteins in action monitored by time-resolved FTIR spectroscopy

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Abstract

In the post genome era proteins coming into the focus of life sciences. X-ray structure analysis and NMR spectroscopy are established methods to determine the geometry of proteins. In order to determine the molecular reaction mechanism of proteins, time-resolved FTIR (trFTIR) difference spectroscopy emerges as a valuable tool. In this Minireview we describe the trFTIR differences spectroscopy and show its application on the light-driven proton pump bacteriorhodopsin (bR), the photosynthetic reaction center and the GTPase Ras, which is crucial in signal transduction. The main principles of the technique are presented, including a summary of triggering techniques, scan modes and analysis. © 2005 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

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Kötting, C., & Gerwert, K. (2005). Proteins in action monitored by time-resolved FTIR spectroscopy. ChemPhysChem, 6(5), 881–888. https://doi.org/10.1002/cphc.200400504

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