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High resolution nuclear magnetic resonance studies of the conformation of luteinizing hormone releasing hormone (LH-RH) and its component peptides
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1973
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Molecular BiologyPeptide ScienceChemical BiologyProtein FoldingBiophysicsProtein ChemistryGrowth HormoneBiochemistryEndocrine MechanismG Protein-coupled ReceptorChemical ShiftsModel PeptidesSolution Nmr SpectroscopyEndocrinologyComponent PeptidesNatural SciencesPeptide TherapeuticReceptor BiologyMedicine
The 1H and 13C n.m.r. spectra of luteinizing hormone releasing hormone (LH-RH) decapeptide, < Glu-His-OMe, <Glu-His-Trp-Ser-Tyr-Gly, Trp-Ser-Tyr-Gly, and Leu-Arg-Pro-GlyNH2 have been studied. In aqueous solution the observed JNC coupling constants are consistent with the molecules being in random coil configurations. There was no evidence for strong intramolecular hydrogen bonding involving CO ⋯ HN The similarities in 1H and 13C chemical shifts between model peptides, the component peptides, and the LH-RH decapeptide suggest no specific side-chain interactions. In particular there is no stacking of the aromatic rings. The 13C chemical shifts of the β- and γ-13C carbons in Pro in LH-RH indicate Pro to be in a trans-configuration.