Solution Conformations of Potent Bicyclic Antagonists of Oxytocin by Nuclear Magnetic Resonance Spectroscopy and Molecular Dynamics Simulations
- 1 June 1997
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 119 (25) , 5833-5846
- https://doi.org/10.1021/ja963736y
Abstract
No abstract availableKeywords
This publication has 44 references indexed in Scilit:
- Conformational and topographical considerations in the design of biologically active peptidesBiopolymers, 1993
- Conformational properties of oxytocin in dimethyl sulfoxide solution: NMR and restrained molecular dynamics studiesBiopolymers, 1992
- Conformational analysis of [Cpp1, Sar7, Arg8] vasopressin by 1H‐NMR spectroscopy and molecular mechanics calculationsInternational Journal of Peptide and Protein Research, 1991
- Conformationally restricted analogs of oxytocin; stabilization of inhibitory conformation†International Journal of Peptide and Protein Research, 1990
- Three-dimensional structure of rabbit liver [Cd7]metallothionein-2a in aqueous solution determined by nuclear magnetic resonanceJournal of Molecular Biology, 1988
- Energy parameters in polypeptides. 9. Updating of geometrical parameters, nonbonded interactions, and hydrogen bond interactions for the naturally occurring amino acidsThe Journal of Physical Chemistry, 1983
- 1,4-Dialkylgermabenzole - Erzeugung und Nachweis in der GasphaseAngewandte Chemie International Edition in English, 1982
- Energy parameters in polypeptides. VII. Geometric parameters, partial atomic charges, nonbonded interactions, hydrogen bond interactions, and intrinsic torsional potentials for the naturally occurring amino acidsThe Journal of Physical Chemistry, 1975
- Vicinal Proton Coupling in Nuclear Magnetic ResonanceJournal of the American Chemical Society, 1963
- ENZYMATIC CLEAVAGE OF GLYCINAMIDE FROM VASOPRESSIN AND A PROPOSED STRUCTURE FOR THIS PRESSOR-ANTIDIURETIC HORMONE OF THE POSTERIOR PITUITARYJournal of the American Chemical Society, 1953