FTIR spectroscopy was used to study the effects of sol-gel encapsulation on the secondary structure of the guest proteins. Gel samples were prepared as KBr pellets and the spectrum of a blank gel was subtracted from that of a doped gel. Proper subtraction yields a spectrum of the pure protein. We explored the amide I/II regions (1700-1500 cm<sup>-1</sup>) of the resultant protein spectrum and compared it with the spectra of lyophilized protein crystals prepared both as KBr pellets and in AgCl discs. Curve fitting was initially applied to the amide I region (1700-1600 cm<sup>-1</sup>) using a carbonyl stretch reference peak obtained from a sample of 3-heptanone. We attempted to identify the amounts and types of secondary structure in the molecule, however, the validity of our results are somewhat tentative due to the difficulty arising from water subtraction within this region. Because the amide II region (1550-1515 cm<sup>-1</sup>) is free from water absorbance, future experiments will be focused on this region.