Symmetry patterns in trypsinogen.
When the primary structure of bovine trypsinogen is searched for the existence of regularities, according to Greller & Erhan (1974), one finds eight pairs of peptides, arranged in a symmetrical pattern along the molecule. These peptides cover 49% of the length of the molecule-112 of the 227 amino acids-and each pair folds in a similar way. This observation is in agreement with the observation that "Trypsin folds into two halves, each of which contains a pseudo-cylindrical arrangement of hydrogen bonds...", Stroud et al. (1971). Thus the above mentioned method is capable not only of detecting regulatities along the primary structure but also of predicting the folding of a protein.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000302:isolation & purification; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D002919:Chymotrypsinogen / Q000032:analysis; D010196:Pancreatic Elastase / Q000032:analysis; D010446:Peptide Fragments / Q000302:isolation & purification; D010455:Peptides / Q000302:isolation & purification; D011487:Protein Conformation; D014362:Trypsinogen / Q000032:analysis*
D000596:Amino Acids; D010446:Peptide Fragments; D010455:Peptides; D014362:Trypsinogen; D002919:Chymotrypsinogen; D010196:Pancreatic Elastase