title: Molecular reaction mechanisms of proteins monitored by time-resolved FTIR-spectroscopy.
abstract: Time-resolved FTIR difference spectroscopy can provide a valuable insight into the molecular reaction mechanisms of proteins, especially membrane proteins. Isotopic labeling and site-directed mutagenesis allows an unequivocal assignment of IR absorption bands. Studies are presented which give insight into the proton pump mechanisms of proteins, especially bacteriorhodopsin. H-bonded network proton transfer via internal water molecules seems to be a general feature in proteins, also found in cytochrome c oxidase. Using caged GTP the intrinsic and GAP catalyzed GTPase activity of H-ras p21 is studied. Furthermore, protein folding reactions can be recorded with ns time-resolution.
authors.affiliation: Ruhr-Universität Bochum, Lehrstuhl für Biophysik, Germany.
authors.forename: K
authors.initials: K
authors.lastname: Gerwert
mesh_terms: D001436:Bacteriorhodopsins / Q000737:chemistry*; D015689:Oncogene Protein p21(ras) / Q000737:chemistry*; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D001436:Bacteriorhodopsins; D015689:Oncogene Protein p21(ras)