[The effect of crystallization of calcium carbonate on the secondary structure of pepsin].
The effect of crystallization of calcium carbonate on the secondary structure of pepsin was studied by Fourier transform infrared spectroscopy, derivative, deconvolution and curve-fitting techniques in this paper. The result shows that the pure protein is composed of 24.38% alpha-helices, 29.91% beta-sheets, 39.22% beta-turns and 6.49% random structures, and the pepsin in the CaCO3/pepsin solution is composed of 2.09% alpha-helices, 93.304% beta-sheets, 4.60% beta-turns and 0.006% random structures. From these data we can see that the alpha-helices decrease and the beta-turns increase with the formation of the crystal of calcium carbonate. The essence of these changes is discussed in the paper.