Abstract
Various methods for examining the infrared spectra of proteins have been investigated using yeast alcohol dehydrogenase and ribonuclease as typical proteins. These methods include films cast from aqueous solutions, KBr disks, and agar films. The effect of preparation method was examined by measuring the enzymic activities of these proteins. The yeast alcohol dehydrogenase loses activity in all cases, and the infrared spectra show that the enzyme is in the stretched or random coil form. Ribonuclease is not denatured as a film but is denatured with the other sampling procedures. However, the spectra indicate no change in the structure of this latter protein. The sampling procedure to be used will depend upon the nature of the protein, and the extent of denaturation of the protein should be checked by an independent method before interpreting its infrared spectrum. Tissue spectra are unreliable for determining the structure of its protein components.
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