Abstract

Fourier self-deconvolution (FSD) has been employed to enhance the resolution of the infrared spectra of proteins in the solid state and in D<sub>2</sub>O solution. The feasibility of using diffuse reflectance spectrometry for measuring the infrared spectra of solid proteins has been demonstrated. FSD permits inherently broad absorption bands to be resolved into distinct peaks which can be associated with specific protein secondary structures. Because the areas of the resolved peaks are the same as the areas of the previously unidentifiable components, this new method should enable quantitative estimates of the proportion of each conformation in a protein to be calculated.

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