title: Optimization of model parameters for describing the amide I spectrum of a large set of proteins.
abstract: A new simulation protocol for the prediction of the infrared absorption of the amide I vibration of proteins was developed. The method incorporates known effects on the intrinsic frequencies (backbone conformation, interpeptide and peptide-solvent hydrogen bonding) and couplings (nearest neighbor coupling, transition dipole coupling) of amide I oscillators in a parametrized manner. Model parameters for the simulation of amide I spectra were determined through fitting and optimization of simulated spectra to experimentally measured infrared spectra of 44 proteins that represent maximum structural variation in terms of different folds and secondary structure contents. Prediction of protein spectra using the optimized parameters resulted in good agreement with experimental spectra and in a considerable improvement compared to a description involving only transition dipole coupling.
authors.affiliation: Department of Biochemistry and Biophysics, Arrhenius Laboratories of Natural Sciences, Stockholm University , SE-106 91, Sweden.
authors.forename: Eeva-Liisa
authors.initials: EL
authors.lastname: Karjalainen
authors.forename: Tore
authors.initials: T
authors.lastname: Ersmark
authors.forename: Andreas
authors.initials: A
authors.lastname: Barth
mesh_terms: D000577:Amides / Q000737:chemistry*; D008958:Models, Molecular; D011506:Proteins / Q000737:chemistry*; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D000577:Amides; D011506:Proteins