Symmetry patterns in trypsinogen.

S Erhan; L D Greller; B Rasco

doi:10.1111/j.1399-3011.1977.tb01831.x

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PubMed · 838530

Symmetry patterns in trypsinogen.

S Erhan·L D Greller·B Rasco

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Abstract

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.

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Amino Acid Sequence Amino Acids Animals Binding Sites Cattle Chemical Phenomena Chemistry Chymotrypsinogen Pancreatic Elastase Peptide Fragments Peptides Protein Conformation Trypsinogen Journal Article

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S Erhan, L D Greller, B Rasco. 1977. Symmetry patterns in trypsinogen.. https://doi.org/10.1111/j.1399-3011.1977.tb01831.x

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