Peptide backbone conformation by solid-state nuclear magnetic resonance spectroscopy
- 1 January 1988
- journal article
- research article
- Published by Royal Society of Chemistry (RSC) in Journal of the Chemical Society, Faraday Transactions 1: Physical Chemistry in Condensed Phases
- Vol. 84 (11) , 3803-3819
- https://doi.org/10.1039/f19888403803
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.This publication has 4 references indexed in Scilit:
- Peptide plane orientations determined by fundamental and overtone nitrogen 14 NMRJournal of the American Chemical Society, 1986
- Protein structure by solid state nuclear magnetic resonanceJournal of Molecular Biology, 1985
- Solid-state NMR of cyclic pentapeptidesJournal of the American Chemical Society, 1985
- Crystal structure of a tripeptide, L‐alanyl‐glycyl‐glycine and its relevance to the poly(glycine)‐II type of conformationBiopolymers, 1983