Conformational studies on polypeptide models of collagen. Poly(Gly-Pro-Val), poly(Gly-Pro-Met), poly(Gly-Val-Pro) and poly(Gly-Met-Pro).
The title polytripeptides were synthesized and studied experimentally, by circular dichroism, and theoretically, by quantum mechanical methods. With the exception of poly(Gly-Pro-Val), which was found to be essentially structureless in solution, the other polymers adopt folded conformations, most probably of type II beta-bends. Conclusions from theoretical studies were generally in agreement with the experimental results. In particular, it is noteworthy that the optimized (phi, psi) maps for poly(Gly-Pro-Met) showed the absolute minimum (phi = 60 degree, psi = 0 degrees) located inside the beta II bend space.
D002942:Circular Dichroism; D003094:Collagen; D008961:Models, Structural; D010455:Peptides / Q000138:chemical synthesis; D011487:Protein Conformation
D010455:Peptides; D003094:Collagen