Abstract
Constant-time dipolar recoupling pulse sequences are advantageous in structural studies by solid state nuclear magnetic resonance (NMR) with magic-angle spinning (MAS) because they yield experimental data that are relatively insensitive to radio-frequency pulse imperfections and nuclear spin relaxation processes. A new approach to the construction of constant-time homonuclear dipolar recoupling sequences is described, based on symmetry properties of the recoupled dipole-dipole interaction Hamiltonian under cyclic displacements in time with respect to the MAS sample rotation period. A specific symmetry-based pulse sequence called PITHIRDS-CT is introduced and demonstrated experimentally. C13 NMR data for singly-C13-labeled amino acid powders and amyloid fibrils indicate the effectiveness of PITHIRDS-CT in measurements of intermolecular distances in solids. N15-detected and C13-detected measurements of intramolecular N15–N15 distances in peptides with α-helical and β-sheet structures indicate the utility of PITHIRDS-CT in studies of molecular conformations, especially measurements of backbone ψ torsion angles in peptides containing uniformly N15- and C13-labeled amino acids.
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Dates
Type | When |
---|---|
Created | 18 years, 6 months ago (Feb. 13, 2007, 6:46 p.m.) |
Deposited | 2 years ago (Aug. 3, 2023, 5:41 a.m.) |
Indexed | 1 month ago (July 30, 2025, 6:48 a.m.) |
Issued | 18 years, 6 months ago (Feb. 13, 2007) |
Published | 18 years, 6 months ago (Feb. 13, 2007) |
Published Online | 18 years, 6 months ago (Feb. 13, 2007) |
Published Print | 18 years, 6 months ago (Feb. 14, 2007) |
@article{Tycko_2007, title={Symmetry-based constant-time homonuclear dipolar recoupling in solid state NMR}, volume={126}, ISSN={1089-7690}, url={http://dx.doi.org/10.1063/1.2437194}, DOI={10.1063/1.2437194}, number={6}, journal={The Journal of Chemical Physics}, publisher={AIP Publishing}, author={Tycko, Robert}, year={2007}, month=feb }