Figure 2.

Protein secondary structure analysis. (a) The representative of the second derivatives of the ATR-FTIR absorbance spectra confined to amide I band. (b) Deconvolution of amide I region: baseline corrected spectra were fitted with six Gaussian band profiles by approximating number and position using the minima of second derivatives, which simulated fits to the experimental curve. Six Gaussian band profiles are assigned as (1) side chain (~1610 cm⁻¹), (2) β sheet (~1630 cm⁻¹), (3) random coil (~1645 cm⁻¹), (4) α helix (~1652 cm⁻¹), (5) β turn (~1682 cm⁻¹) and (6) β anti-parallel sheet (~1690 cm⁻¹) structures. (c) Averaged Gaussian function energy bands of each studied types which prove elevation of β sheet and drop off α helix structures due to malignancies, while other structures remain same.