A comprehensive analysis of crystallographic data of 565 high-resolution protein homodimers comprised of over 250. 000 residues suggests that amino acids form two groups that differ in their tendency to distort or symmetrize the structure of protein homodimers. Residues of the first group tend to distort the protein homodimer and generally have long or polar side chains. These include... https://www.giantrobos.shop/product-category/journals-notepads/