| Literature DB >> 18266429 |
Abstract
The acquisition and analysis of high resolution one- and two-dimensional solid-state nuclear magnetic resonance (NMR) spectra without chemical shift frequencies are described. Many variations of shiftless NMR spectroscopy are feasible. A two-dimensional experiment that correlates the dipole-dipole and dipole-dipole couplings in the model peptide , (15)N labeled N-acetyl-leucine is demonstrated. In addition to the resolution of resonances from individual sites in a single crystal sample, the bond lengths and angles are characterized by the two-dimensional powder pattern obtained from a polycrystalline sample.Entities:
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Year: 2008 PMID: 18266429 PMCID: PMC3760504 DOI: 10.1063/1.2816786
Source DB: PubMed Journal: J Chem Phys ISSN: 0021-9606 Impact factor: 3.488