Evidence from proton magnetic resonance data for the stacking of aromatic amino acids in lysine-vasopressin: Comparison with oxytocin derivatives and related dipeptides
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference12 articles.
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3. Interaction and association of bases and nucleosides in aqueous solutions. V. Studies of the association of purine nucleosides by vapor pressure osmometry and by proton magnetic resonance
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1. Membrane structure and interactions of peptide hormones with model lipid bilayers;Biochimica et Biophysica Acta (BBA) - Biomembranes;2012-12
2. 1H-NMR-Untersuchungen bei 300 MHz zur Wechselwirkung aromatischer Reste in linearen Peptidhormonen;Zeitschrift für Chemie;2010-09-01
3. SPECTROSCOPIC STUDY OF THE CONFORMATIONS OF PROLINE-CONTAINING OLIGOPEPTIDES IN THE CRYSTALLINE STATE AND IN SOLUTION;International Journal of Peptide and Protein Research;2009-01-12
4. Investigation ofcis/trans ratios of peptide bonds in AVP analogues containingN-methylphenylalanine enantiomers;Journal of Peptide Science;2005
5. Conformations of triglycyl-lysylvasopressin:1H NMR spectroscopic and molecular dynamics study;Magnetic Resonance in Chemistry;1993-05
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