Journal article
SYMMETRY PATTERNS IN TRYPSINOGEN
International Journal of Peptide and Protein Research, Vol.9(1), pp.5-10
01/1977
Handle:
https://hdl.handle.net/2376/114891
PMID: 838530
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 regularities along the primary structure but also of predicting the folding of a protein.
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Details
- Title
- SYMMETRY PATTERNS IN TRYPSINOGEN
- Creators
- Semih ErhanLarry D GrellerBarbara Rasco
- Publication Details
- International Journal of Peptide and Protein Research, Vol.9(1), pp.5-10
- Academic Unit
- Food Science, School of
- Publisher
- Blackwell Publishing Ltd; Oxford, UK
- Number of pages
- 6
- Identifiers
- 99900547874801842
- Language
- English
- Resource Type
- Journal article