[The content of alpha-helix and beta-structure in proteins crystallized at different pH values].

Using the data of X-ray diffraction analysis for 100 three-dimensional structures of 26 proteins uniformly distributed among three main classes of the alpha-helix-beta-structure classification and without potentially polyanion regions, 154 comparisons of the content of alpha-helix and beta-structure content were made for structures obtained at different pH values of the medium, being distributed in the whole among all these proteins in the range from 1.5 to 12.0. No significant influence of pH of the medium on the size and localization of alpha-helices and beta-strands was found. As a consequence, it is suggested for the protein structure in a crystal that the alpha-helical-beta-structural backbone of protein structures does not depend on pH of the medium, except when the whole protein or its part can become a polyion so that the electrostatic interactions would either hinder or favour the formation of regular structures, and the conformational properties of ionizable amino acids are independent of pH of the medium. It is unclear, whether these assumptions can be extended to the case of solution, because the data for the structures in solution have been obtained for one protein only. These results can be used in investigations of protein structure, in protein engineering, and in the creation of specialized data banks of protein structures.