phoagy Lv 1
Can you set up phosphoserine peptides that might help in modeling casein, a protein that does not want to fold into minimized crystalizable structures that can be crystallized? The phosphoserine residue by itself is restrained by a weak hydrogen bond between the gamma O and the alpha NH of the PSE (personal observation). The phosphate O's disrupt downstream backbone H-bonds. In addition, internal salt bridges with Lys or Arg are possible strong interactions. I am a retired chemist who did limited molecular modeling of some casein components and model phoshopetides. Your fold.it program is great! I like the way you have restricted the movement of side chains to reasonable angles.
