Abstract

In an FT-IR study of the secondary structure of proteins, several concentrations, cell pathlengths, resolution values, and machine parameters were investigated. During this investigation we observed that 1-cm⁻¹ resolution spectra of hemoglobin enhanced by second derivatives revealed an additional band in the α-helix region. Krimm and co-workers predicted the existence of two absorbances in the infrared amide I region (1600-1700 cm⁻¹) of α-helical proteins in solution that correspond to the <i>A</i> and <i>E</i>₁ amide carbonyl vibrational modes. However, they observed only one band in the α-helix region at 2 cm⁻¹ resolution.

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