In magic angle spinning (MAS) NMR recoupling experiments, the extraction of multiple couplings or a coupling distribution from the observed dephasing signals remains a challenging problem. At least for REDOR experiments, the REDOR transform solves this problem, enabling the simultaneous measurement of multiple dipolar couplings. Focusing on the quadrupolar dephasing observed in QUADRAMA experiments as a representative example, we demonstrate that the same analytical form used for the mathematical description of REDOR dephasing also describes the dephasing observed in a wide variety of MAS NMR recoupling experiments. This fact immediately extends REDOR transform techniques to a much broader suite of recoupling experiments than had previously been realized, including those of DRAMA, MELODRAMA and QUADRAMA. As an illustration, we use the DRAMAtic transform to provide the first inversion of a QUADRAMA dephasing signal to extract the quadrupole coupling distribution. Using a complete elliptic integral of the first kind, we further develop a novel expression for the Pake-spun powder patterns of the corresponding recoupled lineshapes. Our methods and results reinforce the central role that Bessel functions can play in simplifying the integrals that define both the dephasing signals in the time domain, and their Fourier transforms in the frequency domain.
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http://dx.doi.org/10.1016/j.ssnmr.2005.03.001 | DOI Listing |
J Phys Chem A
January 2025
Department of NMR based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Am Faßberg 11, Göttingen 37077, Germany.
Theoretical and simulated analyses of selective homonuclear dipolar recoupling sequences serve as primary tools for understanding and determining the robustness of these sequences under various conditions. In this article, we investigate the recently proposed first-order dipolar recoupling sequence known as MODIST (Modest Offset Difference Internuclear Selective Transfer). We evaluate the MODIST transfer efficiency, assessing its dependence on rf-field strengths and the number of simulated spins, extending up to 10 spins.
View Article and Find Full Text PDFBiophys J
January 2025
Departement of Chemistry, Université du Québec à Montréal, Montreal, Québec, Canada. Electronic address:
Fluorine-19 is an ideal nucleus for studying biological systems using NMR due to its rarity in biological environments and its favorable magnetic properties. In this work, we used a mixture of monofluorinated palmitic acids (PAs) as tracers to investigate the molecular interaction of the fluorinated drug rosuvastatin in model lipid membranes. More specifically, PAs labeled at the fourth and eighth carbon positions of their acyl chains were coincorporated in phospholipid bilayers to probe different depths of the hydrophobic core.
View Article and Find Full Text PDFJ Magn Reson
November 2024
Department of Chemistry and Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology, Cambridge, MA 02139, United States. Electronic address:
In magic angle spinning (MAS) experiments involving uniformly C/N labeled proteins, C-C and C-N dipolar recoupling experiments are now routinely used to measure direct dipole-dipole couplings that constrain distances and torsion angles and determine molecular structures. When the distances are short (<4 Å), the direct couplings dominate the evolution of the spin system, and the C-C and C-N J-couplings (scalar couplings) are ignored. However, for structurally interesting >4 Å distances, the dipolar and J-couplings are generally of comparable magnitude, and the variation in J must be included in order to optimize the precision of the experiment.
View Article and Find Full Text PDFJACS Au
September 2024
School of Chemistry, Faculty of Exact sciences, Tel Aviv University, Tel Aviv 6997801, Israel.
The development of robust NMR methodologies to probe dynamics on the atomic scale is vital to elucidate the close relations between structure, motion, and function in biological systems. Here, we present an automated protocol to measure, using magic-angle spinning NMR, the effective C-N dipolar coupling constants between multiple spin pairs simultaneously with high accuracy. We use the experimental dipolar coupling constants to quantify the order parameters of multiple C-N bonds in the thousands of identical copies of the coat protein in intact fd-Y21M filamentous bacteriophage virus and describe its overall dynamics on the submillisecond time scale.
View Article and Find Full Text PDFChemphyschem
December 2024
Polymer Science and Technology, CSIR-Central Leather Research Institute, Adyar, Chennai, 600020, India.
A Model mesogen and its symmetrical Dimer made up of phenyl benzoate core unit are investigated by C NMR spectroscopy. The existence of layer order in smectic A and smectic C phases of Dimer mesogen is established by powder X-ray diffraction. The chemical shift anisotropy (CSA) tensors of Model mesogen are determined by 2D separation of undistorted powder patterns by effortless recoupling (SUPER) experiment and are utilized for calculating the order parameters employing the alignment-induced chemical shifts (AIS).
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