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Proteins in Action Monitored by Time‐Resolved FTIR Spectroscopy
Author(s) -
Kötting Carsten,
Gerwert Klaus
Publication year - 2005
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.200400504
Subject(s) - bacteriorhodopsin , spectroscopy , fourier transform infrared spectroscopy , chemistry , infrared spectroscopy , nuclear magnetic resonance spectroscopy , gtpase , analytical chemistry (journal) , stereochemistry , biochemistry , organic chemistry , optics , physics , quantum mechanics , membrane
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 difference 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.