Fourier Transform Infrared Spectroscopy Investigations of Protein Structure

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Abstract
It has been recognized since 1950 (Elliott and Ambrose, 1950) that infrared spectroscopy has the potential to provide information regarding protein secondary structure. Krimm lists nine protein-sensitive infrared active vibrations arising from the amide backbone linkage (Krimm and Bandekar, 1986). The majority of protein structural information, however, has been obtained from one absorbance originating primarily from the amide C=O stretching vibrations: the amide I band. The sensitivity to variations in both geometric arrangement of atoms and hydrogen bonding enables infrared spectroscopy to discriminate between the various secondary structures, i. e., helical, extended sheet, unordered, and turns, incorporated within the three-dimensional organization of peptides and proteins. Many studies have demonstrated, both theoretically and experimentally, that infrared spectroscopy can be used to identify specific secondary structures.

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