Proteins in action monitored by time-resolved FTIR spectroscopy.
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.
Kötting
Carsten
C
Lehrstuhl für Biophysik, ND 04/596, Ruhr-Universität Bochum, 44801 Bochum, Germany. koetting@bph.rub.de
Gerwert
Klaus
K
D001436:Bacteriorhodopsins / Q000737:chemistry*; D020558:GTP Phosphohydrolases / Q000737:chemistry; D006860:Hydrogen Bonding; D007700:Kinetics; D008027:Light; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008956:Models, Chemical; D008958:Models, Molecular; D015233:Models, Statistical; D008968:Molecular Conformation; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry; D015398:Signal Transduction; D013053:Spectrophotometry; D013055:Spectrophotometry, Infrared; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods*; D013997:Time Factors; D014965:X-Rays
D011506:Proteins; D001436:Bacteriorhodopsins; D020558:GTP Phosphohydrolases