correction to peak finding, peak integration, peak deconvolution and fitting. Correction, Smoothing, Spectral derivatives, Deconvolution, Curvefitting, Spectral. in the FTIR spectrum of osteomyelitis tissue, however, the absorbance at 1540 cm1, was greatest, whilst in the FTIR spectra of the ES bone tissue, the highest value of peaks at 2848 cm1, 2916 cm 1, 2956 cm 1, were observed. Column & Bar Charts: Basic, Stacked, Grouped Floating Column & Bar Charts. Small amounts of high-purity (>95%) proteins at high concentrations (>3 mg ml −1) are needed in this protocol typically, the procedure can be completed in 1–2 d. form the fundamental basis for the improved performance of FTIR. In this protocol, we have detailed the principles that underlie the determination of protein secondary structure by FTIR spectroscopy, as well as the basic steps involved in protein sample preparation, instrument operation, FTIR spectra collection and spectra analysis in order to estimate protein secondary-structural components in aqueous (both H 2O and deuterium oxide (D 2O)) solution using algorithms, such as second-derivative, deconvolution and curve fitting.
Amide I bands (1,700–1,600 cm −1) are the most prominent and sensitive vibrational bands of the protein backbone, and they relate to protein secondary structural components. The repeat units in proteins give rise to nine characteristic IR absorption bands (amides A, B and I–VII). The IR spectral data of polymers are usually interpreted in terms of the vibrations of a structural repeat. Fourier transform IR (FTIR) spectroscopy is a nondestructive technique for structural characterization of proteins and polypeptides.