A NOTE ON THE TWO‐DIMENSIONAL REPRESENTATION OF HYDROGEN BONDING SCHEME IN TRIOSE PHOSPHATE ISOMERASE*
- 1 February 1977
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 9 (2) , 157-160
- https://doi.org/10.1111/j.1399-3011.1977.tb03475.x
Abstract
When the backbone hydrogen bonding scheme of the protein triose phosphate isomerase is represented in the two-dimensional map where the donor residue number (i) is taken along the x-axis and the acceptor residue number (j) is taken along the y-axis, the (i, j)-map shows a characteristic pattern of (βα)8-supersecondary structure.This publication has 8 references indexed in Scilit:
- NEW 2-DIMENSIONAL REPRESENTATION OF HYDROGEN-BONDING SCHEME IN PROTEINS1976
- Some new methods and general results of analysis of protein crystallographic structural dataJournal of Molecular Biology, 1975
- Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5Å resolution: using amino acid sequence dataNature, 1975
- A two-dimensional representation of protein structuresArchives of Biochemistry and Biophysics, 1975
- Recognition of structural domains in globular proteinsJournal of Molecular Biology, 1974
- Structure of crystalline α-chymotrypsinJournal of Molecular Biology, 1972
- The Three-Dimensional Structure of Ribonuclease-SJournal of Biological Chemistry, 1970
- Stereochemistry of polypeptide chain configurationsJournal of Molecular Biology, 1963