The 310helical conformation of a pentapeptide containing α-aminoisobutyric acid (Aib): X-ray crystal structure of Tos–(Aib)5–OMe
- 1 January 1978
- journal article
- research article
- Published by Royal Society of Chemistry (RSC) in Journal of the Chemical Society, Chemical Communications
- No. 22,p. 996-997
- https://doi.org/10.1039/c39780000996
Abstract
The pentapeptide Tos–(Aib)5–OMe adopts a 310 helical conformation in the solid state, with three consecutive Type III β-turns stabilised by intramolecular hydrogen bonds.This publication has 4 references indexed in Scilit:
- High resolution and field desorption mass spectrometry studies and revised structures of alamethicins I and IIJournal of the American Chemical Society, 1977
- The crystal and molecular structure of the amino terminal tetrapeptide of alamethicin. A novel 310 helical conformationBiochemical and Biophysical Research Communications, 1977
- Structural and membrane modifying properties of suzukacillin, a peptide antibiotic related to alamethicinBiochimica et Biophysica Acta (BBA) - Biomembranes, 1976
- Chemical nature and sequence of alamethicinBiochemical Journal, 1976