Three-dimensional solid-state NMR spectroscopy of a peptide oriented in membrane bilayers. J Biomol NMR 1995 Nov;6(3):329-34
Date
11/01/1995Pubmed ID
8520224Pubmed Central ID
PMC3282056DOI
10.1007/BF00197814Scopus ID
2-s2.0-0029398795 (requires institutional sign-in at Scopus site) 74 CitationsAbstract
A three-dimensional 1H chemical shift/1H-15N dipolar coupling/15N chemical shift correlation spectrum was obtained on a sample of specifically 15N-labeled magainin peptides oriented in lipid bilayers between glass plates in a flat-coil probe. The spectrum showed complete resolution of the resonances from two labeled amide sites in all three dimensions. The three orientationally dependent frequencies associated with each resonance enabled the orientation of the peptide planes to be determined relative to the direction of the applied magnetic field. These results demonstrate the feasibility of multiple-pulse spectroscopy in a flat-coil probe, the ability to measure three spectral parameters from each site in a single experiment, and the potential for resolving among many labeled sites in oriented membrane proteins.
Author List
Ramamoorthy A, Marassi FM, Zasloff M, Opella SJAuthor
Francesca M. Marassi PhD Chair, Professor in the Biophysics department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
AmidesAmino Acid Sequence
Lipid Bilayers
Magnetic Resonance Spectroscopy
Molecular Sequence Data
Peptides
Protein Conformation
