An infrared and circular dichroism combined approach to the analysis of protein secondary structure.
Selected regions of infarred (ir) and circular dichroism (CD) spectral data from 10 proteins were combined and analyzed by a factor analysis method. The regions consisted of the area normalized amide I region from 1700 to 1600 cm-1 for the ir spectra and from 178 to 240 nm for the CD spectra. Each CD spectrum was scaled by a factor of 0.5 before appending the data to the ir spectral data. The scaling factor was deemed necessary to account for relative intensity differences between the ir and CD data and provided nearly optimum agreement between secondary structure estimated by the combined approach to secondary structure determined by X-ray crystallography. The ir/CD combined approach to estimation of helix, beta-sheet, beta-turn, and other or undefined secondary structure agreed with X-ray crystallographic determined structure better than estimation using data from either method alone. Correlation coefficients between X-ray and ir/CD combined secondary structure determinations were 0.99 for helix, 0.90 for beta-sheet, 0.70 for beta-turn, and 0.78 for other structure. The four most significant eigenvectors or basis spectra from eigenanalysis of the ir/CD data are presented as well as generalized inverse spectra for four secondary structures.
Sarver
R W
RW
Department of Physical and Analytical Chemistry, Upjohn Company, Kalamazoo, Michigan 49001.
Krueger
W C
WC
D002942:Circular Dichroism; D004798:Enzymes / Q000737:chemistry; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D013055:Spectrophotometry, Infrared / Q000379:methods; D014961:X-Ray Diffraction
D004798:Enzymes; D011506:Proteins