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Conformational study of three endothelin antagonists with 1H NMR at low temperature and molecular dynamics
P Verheyden1, I Van Assche, M H Brichard
1Department of Organic Chemistry, Vrije Universiteit Brussel, Belgium.
FEBS Letters
|May 9, 1994
Abstract:
The conformations of three endothelin antagonists, a cyclic pentapeptide, a linear tripeptide and a linear hexapeptide, are compared by 1H NMR and molecular dynamics. The three analogues have a Leu and a DTrp side chain which are oriented parallel, and an acidic group next to the DTrp residue.