The constrained, iterative Fourier deconvolution procedure was applied to quantitatively analyze the overlapped bands in the Raman spectra of biomolecules. When applied to Raman spectra of lysozyme and ${alpha}$-amylase, this procedure resolved the amide Ⅰ band into five component peaks. The relative intensities of the resolved peaks can possibly provide the composition of secondary structure elements in proteins. The deconvolution procedure was also useful in monitoring the small changes in relative intensities of C-S stretching modes due to different conformers of L-methionine in aqueous solutions at different pH values. The implemented procedure is generally applicable to the problem of resolution enhancement of spectroscopic, chromatographic, and electrophoretic data.