The receptor binding affinity of monocyclic [Ala3, Xaa11]endothelin-1 analogs correlates with inducible helix length
- 1 February 1995
- journal article
- Published by Elsevier in Bioorganic & Medicinal Chemistry
- Vol. 3 (2) , 113-124
- https://doi.org/10.1016/0968-0896(95)00005-2
Abstract
No abstract availableKeywords
This publication has 56 references indexed in Scilit:
- Does the solid‐state structure of endothelin‐1 provide insights concerning the solution‐state conformational equilibrium?FEBS Letters, 1994
- Helix propensities of the amino acids measured in alanine‐based peptides without helix‐stabilizing side‐chain interactionsProtein Science, 1994
- Peptide/protein structure analysis using the chemical shift index method: Upfield α-CH values reveal dynamic helices and αL sitesBiochemical and Biophysical Research Communications, 1992
- Importance of secondary structure for endothelin binding and functional activityBiochemical and Biophysical Research Communications, 1992
- [Ala1,3,11,15]endothelin-1 analogs with ETB agonistic activityBiochemical and Biophysical Research Communications, 1991
- The conformation of endothelin-1 in aqueous solution: NMR-Derived constraints combined with distance geometry and molecular dynamics calculationsBiochemical and Biophysical Research Communications, 1991
- Conformation of endothelin in aqueous ethylene glycol determined by1H-NMR and molecular dynamics simulationsFEBS Letters, 1991
- Evidence for aggregation of endothelin 1 in waterFEBS Letters, 1990
- Structure-activity relationships of endothelin: Importance of the C-terminal moietyBiochemical and Biophysical Research Communications, 1988
- Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroismJournal of Molecular Biology, 1980