Insight into protein structure and protein-ligand recognition by Fourier transform infrared spectroscopy.
An overview of the application of Fourier transform infrared spectroscopy for the analysis of the structure of proteins and protein-ligand recognition is given. The principle of the technique and of the spectra analysis is demonstrated. Spectral signal assignments to vibrational modes of the peptide chromophore, amino acid side chains, cofactors and metal ligands are summarized. Several examples for protein-ligand recognition are discussed. A particular focus is heme proteins and, as an example, studies of cytochrome P450 are reviewed. Fourier transform infrared spectroscopy in combination with the various techniques such as time-resolved and low-temperature methods, site-directed mutagenesis and isotope labeling is a helpful approach to studying protein-ligand recognition.
Jung
C
C
Max-Delbrück-Center for Molecular Medicine, Berlin, Germany. cjung@mdc-berlin.de
D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry / Q000378:metabolism; D006418:Heme / Q000737:chemistry / Q000378:metabolism; D008024:Ligands; D011485:Protein Binding; D011487:Protein Conformation; D017550:Spectroscopy, Fourier Transform Infrared
D008024:Ligands; D006418:Heme; D003577:Cytochrome P-450 Enzyme System