Vibrational circular dichroism of polypeptides. 9. A study of chain length dependence for 310-helix formation in solution
- 1 August 1986
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 108 (16) , 4988-4993
- https://doi.org/10.1021/ja00276a046
Abstract
No abstract availableKeywords
This publication has 18 references indexed in Scilit:
- Vibrational circular dichroism of polypeptides. II. Solution amide II and deuteration resultsBiopolymers, 1984
- Circular dichroism studies of helical oligopeptides: Can 310 and α‐helical conformations be chiroptically distinguished?International Journal of Peptide and Protein Research, 1983
- Conformational analysis of linear peptides. 4. Association properties of protected oligomers of .alpha.-aminoisobutyric acid in chloroformJournal of the American Chemical Society, 1983
- Peptaibol antibiotics: Conformational preferences of synthetic emerimicin fragmentsBiopolymers, 1983
- A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-Å resolutionNature, 1982
- Vibrational circular dichroism in amino acids and peptides. 7. Amide stretching vibrations in polypeptidesBiopolymers, 1982
- Aggregation of apolar peptides in organic solvents. Concentration dependence of 1H‐nmr parameters for peptide NH groups in 310 helical decapeptide fragment of suzukacillinBiopolymers, 1982
- Linear oligopeptides. 81. Solid-state and solution conformation of homooligo(.alpha.-aminoisobutyric acids) from tripeptide to pentapeptide: evidence for a 310 helixJournal of the American Chemical Society, 1982
- Sensitivity of polypeptide conformation to geometry. Theoretical conformational analysis of oligomers of .alpha.-aminoisobutyric acidJournal of the American Chemical Society, 1981
- Crystal structures and conformational calculations of fragments of alamethicin containing aminoisobutyric acidJournal of the American Chemical Society, 1981