Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5Å resolution: using amino acid sequence data
Abstract
Each subunit of triose phosphate isomerase is composed of alternate segments of polypeptide chain in the α- and β-conformations that are arranged to form an inner cylinder of parallel-pleated sheet and a largely helical outer shell. Residues participating in the subunit interface and the active sites have been identified.
- Publication:
-
Nature
- Pub Date:
- June 1975
- DOI:
- 10.1038/255609a0
- Bibcode:
- 1975Natur.255..609B