Dilute spin-exchange assignment of solid-state NMR spectra of oriented proteins: Acetylcholine M2 in bilayers
Source: Journal of Biomolecular NMR, Volume 14, Number 2, June 1999 , pp. 141-148(8)
Abstract: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.
Document Type: Regular Paper
Publication date: June 1, 1999