Extended Helical Conformation Newly Observed in Protein Folding
- 12 November 1976
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 194 (4266), 720-722
- https://doi.org/10.1126/science.982035
Abstract
A new secondary structure, which shows regularity within the experimental error, is noticed in alpha-chymotrypsin, and considering its extended nature, the name epsilon-helix has been suggested for the same. The average observed values of phi and psi for this conformation are -93 degrees and +146 degrees, respectively. The helical parameters turn out to be n = 2.7 and h = 3.3 angstroms.This publication has 3 references indexed in Scilit:
- Some new methods and general results of analysis of protein crystallographic structural dataJournal of Molecular Biology, 1975
- Structure of crystalline α-chymotrypsinJournal of Molecular Biology, 1972
- Conformation of Polypeptides and ProteinsAdvances in protein chemistry, 1968