Proton Magnetic Resonance Study of Peptide Conformation: Effect of Trifluoroethanol on Oxytocin and 8-Lysine-Vasopressin
AUTOR(ES)
Walter, Roderich
RESUMO
The usefulness of 2,2,2-trifluoroethanol titration as a means of distinguishing between intramolecular peptide-peptide hydrogen bonding on the one hand and intermolecular peptide-peptide and peptide-solvent hydrogen bonding on the other has been investigated with neurohypophyseal hormones, and the results have been compared with those of other methods. The chemical shifts (220 MHz) of the resonances of amide NH and aromatic CH protons of oxytocin, lysine vasopressin, deamino-lysine vasopressin, and deamino-8-tosyllysine vasopressin were monitored as the solvent composition was progressively varied from 100% dimethylsulfoxide to 100% 2,2,2-trifluoroethanol. The overall backbone conformation of oxytocin appears to be retained, and possibly somewhat stabilized, during the solvent transition, while the backbone, particularly the acyclic component, of lysine vasopressin and its analogs is subject to solvent-induced perturbation.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=433457Documentos Relacionados
- Nuclear Magnetic Resonance Studies of Lysine-Vasopressin: Structural Constraints
- Nuclear Magnetic Resonance Spectrum of Lysine-Vasopressin and Its Structural Implications
- Nuclear Magnetic Resonance Spectrum of Lysine-Vasopressin in Aqueous Solution and Its Structural Implications
- Proton Magnetic Resonance Comparison of Neurohypophyseal Hormones and Analogs: Deletion of Amino Groups and the Conformation of Lysine Vasopressin
- Method for Correlation of Proton Magnetic Resonance Assignments in Different Solvents: Conformational Transition of Oxytocin and Lysine Vasopressin from Dimethylsulfoxide to Water