Nuclear Magnetic Resonance Studies of Lysine-Vasopressin: Structural Constraints
AUTOR(ES)
Von Dreele, P. H.
RESUMO
The 220-MHz proton NMR spectra of lysine-vasopressin and some related compounds are examined in deuterated dimethyl sulfoxide to obtain structural information that must be satisfied by any proposed conformation of the molecule. This structural information is in the form of dihedral angles (for rotation about the NH-CαH bonds) from coupling constants, possible hydrogen bonding of the CONH2 and backbone amide groups from the temperature-dependence of the chemical shift, and aromatic ring-aromatic ring interaction from the effect of the magnetically anisotropic groups on the chemical shift.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=389596Documentos Relacionados
- 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 Study of Peptide Conformation: Effect of Trifluoroethanol on Oxytocin and 8-Lysine-Vasopressin
- Nuclear Magnetic Resonance Spectrum of Deamino-Lysine-Vasopressin in Aqueous Solution and Its Structural Implications
- Conformational Studies of Oxytocin, Lysine Vasopressin, Arginine Vasopressin, and Arginine Vasotocin by Carbon-13 Nuclear Magnetic Resonance Spectroscopy
