Dilute spin-exchange assignment of solid-state NMR spectra of oriented proteins: acetylcholine M2 in bilayers. J Biomol NMR 1999 Jun;14(2):141-8
Date
07/31/1999Pubmed ID
10427741Pubmed Central ID
PMC3282054DOI
10.1023/a:1008391823293Scopus ID
2-s2.0-0033059428 (requires institutional sign-in at Scopus site) 45 CitationsAbstract
The assignment of amide resonances in the two-dimensional PISEMA (Polarization Inversion with Spin Exchange at the Magic Angle) spectrum of uniformly 15N labeled M2 peptide corresponding to the channel-lining segment of the acetylcholine receptor in oriented phospholipid bilayers is described. The majority of the resonances were assigned through comparisons with spectra from selectively 15N labeled recombinant peptides and specifically 15N labeled synthetic peptides. Some resonances were assigned to specific amino acid residues by means of homonuclear 15N spin-exchange spectroscopy. A modification to the conventional spin-exchange pulse sequence that significantly shortens the length of the experiments by combining the intervals for 15N spin-exchange and 1H magnetization recovery is described.
Author List
Marassi FM, Gesell JJ, Valente AP, Kim Y, Oblatt-Montal M, Montal 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
Amino Acid SequenceLipid Bilayers
Molecular Sequence Data
Nitrogen Isotopes
Nuclear Magnetic Resonance, Biomolecular
Peptide Fragments
Protein Conformation
Receptor, Muscarinic M2
Receptors, Muscarinic
