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Insight into protein structure and protein–ligand recognition by Fourier transform infrared spectroscopy
Author(s) -
Jung Christiane
Publication year - 2000
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/1099-1352(200011/12)13:6<325::aid-jmr507>3.0.co;2-c
Subject(s) - chemistry , fourier transform infrared spectroscopy , fourier transform , ligand (biochemistry) , infrared spectroscopy , spectroscopy , chromophore , protein structure , crystallography , photochemistry , biochemistry , organic chemistry , physics , optics , receptor , quantum mechanics
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. Copyright © 2000 John Wiley & Sons, Ltd. Abbreviations used: Adx adrenodoxinATP adenosine 5′‐triphosphateCD circular dichroismDHAP dihydroxyacetone phosphateFTIR Fourier transform infrared spectroscopyGAP D ‐glyceraldehyde 3‐phosphatePdx putidaredoxinP450 cytochrome P450P450cam P450 from camphor‐hydroxylating Pseudomonas putida .