Abstract
Secondary structure breakers, particularly hairpin structures, impose strong limitations on the global structure of a protein. Three kinds of secondary structure breakers (proline, glycine and amphiphilic residues) were studied in myoglobin and hemoglobin, which are typical all-α type proteins. Secondary structure breakers were located as predicted in about two thirds of the interhelical loops. Charge symmetry analysis provided evidence that high charge symmetry drives the formation of hairpin structures. Based on this information about breakers and hairpin structures, the possibility of folding a protein in silico is discussed.
