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Spin systems where the difference in chemical shifts of the coupled nuclei is greater than ten times J are called first-order spin systems. These nuclei are weakly coupled, and their chemical shifts and coupling constant can generally be estimated from the well-separated signals in the spectrum.
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At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
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Heteronuclear single-quantum correlation spectroscopy (HSQC) is a 2D NMR technique that reveals one-bond correlations between hydrogen and a heteronucleus. The HSQC experiment is similar to the heteronuclear correlation experiment (HETCOR) but is more sensitive. In the HSQC spectrum, the proton chemical shift is plotted on the horizontal F2 axis, while the 13C chemical shift is plotted on the vertical F1 axis. The corresponding proton and 13C spectra are also shown. The HSQC contour plot does...
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Two-Dimensional (2D) NMR: Overview01:12

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The 1D NMR spectrum of large and complex molecules like natural products has complicated splitting patterns and overlapping signals, which can be easily interpreted using 2-dimensional (2D) NMR. Unlike 1D NMR, 2D NMR has two frequency axes that provide the coupling information between the nucleus A and nucleus B in a molecule. The process from which 2D spectra are obtained has four steps.
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In the AX proton spin system, proton A can sense the two spin states of a coupled proton X, resulting in a doublet NMR signal with two peaks of equal (1:1) intensity. When proton A is coupled to two equivalent protons (AX2 spin system), the spin states of each X can be aligned with or against the external field, creating three possible scenarios. This results in a 1:2:1  triplet signal, where the central peak corresponds to the chemical shift of A and is twice as large or intense as the...
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Line Shape Analysis of Dynamic NMR Spectra for Characterizing Coordination Sphere Rearrangements at a Chiral Rhenium Polyhydride Complex
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Protein dynamics in the solid state from 2H NMR line shape analysis: a consistent perspective.

Eva Meirovitch1, Zhichun Liang, Jack H Freed

  • 1The Mina and Everard Goodman Faculty of Life Sciences, Bar-Ilan University , Ramat-Gan 52900, Israel.

The Journal of Physical Chemistry. B
|January 17, 2015
PubMed
Summary
This summary is machine-generated.

We developed a new method for deuterium NMR line shape analysis to study protein dynamics. This approach, based on the microscopic-order-macroscopic-disorder model, allows for better comparison across different protein systems.

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Area of Science:

  • Solid-state Nuclear Magnetic Resonance (NMR) Spectroscopy
  • Protein Dynamics
  • Computational Biophysics

Background:

  • Deuterium (2H) line shape analysis of CD3 groups is valuable for studying protein motions on microsecond-millisecond timescales in the solid state.
  • Existing models are often case-specific, limiting cross-system comparisons and requiring model modifications for improvements.

Purpose of the Study:

  • To develop a novel, generalized methodology for (2H) NMR line shape analysis that overcomes the limitations of previous case-specific models.
  • To enable robust comparisons of protein dynamics across different systems.

Main Methods:

  • Implementation of the microscopic-order-macroscopic-disorder (MOMD) approach to describe motions using diffusion tensors, potentials/ordering tensors, and relative tensor orientations.
  • Recovery of jump-type motions in the limit of large orientational potentials.
  • Model improvement through monitoring tensor magnitude, symmetry, and orientation.

Main Results:

  • Successfully reproduced CD3 line shapes from Chicken Villin Headpiece Subdomain and Streptomyces Subtilisin Inhibitor using the MOMD approach.
  • Identified rhombic local potentials (L=2 spherical harmonics) and axial diffusion tensors.
  • Determined potential strength and rhombicity (ca. 2-3 kBT), diffusion tensor tilt (120° from C-CD3 axis), and correlation times (0.1-1.0 ms perpendicular, 3.3-30 μs parallel).
  • Estimated activation energies in the range of 1.1-8.0 kcal/mol.

Conclusions:

  • The developed MOMD methodology provides a versatile and generalizable framework for (2H) NMR line shape analysis of protein dynamics.
  • This approach facilitates direct comparisons between different protein systems and offers insights into motional parameters.
  • Future work includes extension to relaxation measurements, other NMR nuclei, and complex media.