Peptide backbone conformation by solid-state nuclear magnetic resonance spectroscopy
Abstract
Solid-state 14N NMR spectroscopy is used to determine the backbone structure of the peptides N-acetyl-L-valyl-L-leucine and L-alanylglycyl-glycine in single crystals. These samples provide examples of both glycyl and non-glycyl residues in peptide linkages. There is good agreement between the structures determined by solid-state NMR spectroscopy and X-ray diffraction, demonstrating that solid-state NMR spectroscopy can describe peptide backbone structures without the use of isotopic labels.
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