Conformational studies on sequential polypeptides Part VI. Structural investigations on (Pro-Leu-Gly)10, (Pro-Leu-Gly)n and (Leu-Pro-Gly)n.
The conformational properties of (Pro-Leu-Gly)10, (Pro-Leu-Gly)n and (Leu-Pro-Gly)n were investigated both in solution and in solid state. By circular dichroism studies it was possible to demonstrate the formation of an ordered collagen-like structure for (Pro-Leu-Gly)n in hexafluroisopropanol-water mixtures and in ethylene glycol; (Leu-Pro-Gly)n assumes an ordered conformation only in ethylene glycol; (Pro-Leu-Gly)10 is unordered under all the conditions studied. X-ray diffraction patterns indicated that (Pro-Leu-Gly)n and (Leu-Pro-Gly)n assume a triple helical structure in solid state. In addition, the investigation of (Pro-Leu-Gly)n strongly suggests that this type of structure is a single chain triple helix. The X-ray patterns of (Pro-Leu-Gly)10 do not allow us to ascertain a collagen or polyproline II-like structure for this decatripeptide.
D000595:Amino Acid Sequence; D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D002942:Circular Dichroism; D003094:Collagen; D005998:Glycine; D007930:Leucine; D010455:Peptides; D011392:Proline; D011487:Protein Conformation; D051381:Rats; D014961:X-Ray Diffraction
D010455:Peptides; D003094:Collagen; D011392:Proline; D007930:Leucine; D005998:Glycine