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Related Concept Videos

NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

The spin state of an NMR-active nucleus can have a slight effect on its immediate electronic environment. This effect propagates through the intervening bonds and affects the electronic environments of NMR-active nuclei up to three bonds away; occasionally, even farther. This phenomenon is called spin–spin coupling or J-coupling. Coupling interactions are mutual and result in small changes in the absorption frequencies of both nuclei involved. While nuclei of the same element are involved in...
¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR

The axial and equatorial protons in cyclohexane can be distinguished by performing a variable-temperature NMR experiment. In this process, except for one proton, the remaining eleven protons are replaced by deuterium. The deuterium substitution avoids the possible peak splitting caused by the spin-spin coupling between the adjacent protons. The remaining proton flips between the axial and equatorial positions.
¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

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.
As Δν decreases and the signals move closer, the doublets appear increasingly distorted. The intensities of the inner lines increase at the cost of those of the outer lines as the signals are slanted or...
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

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...
Protein Folding01:22

Protein Folding

Overview
NMR Spectrometers: Resolution and Error Correction01:14

NMR Spectrometers: Resolution and Error Correction

When magnetic nuclei in a sample achieve resonance and undergo relaxation, the signal detected in NMR is an approximately exponential free induction decay. Fourier transform of an exponential decay yields a Lorentzian peak in the frequency domain. Lorentzian peaks in an NMR spectrum are defined by their amplitude, full width at half maximum, and position, where the peak width is governed by the spin-spin relaxation time alone. In real experiments, however, the applied magnetic field is rendered...

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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Protein fold determined by paramagnetic magic-angle spinning solid-state NMR spectroscopy.

Ishita Sengupta1, Philippe S Nadaud, Jonathan J Helmus

  • 1Department of Chemistry, The Ohio State University, 100 West 18th Avenue, Columbus, Ohio 43210, USA.

Nature Chemistry
|April 24, 2012
PubMed
Summary

This study introduces a new method using paramagnetic relaxation enhancements (PREs) to determine protein structures in solid-state NMR. This approach overcomes limitations of traditional methods for challenging biomacromolecules.

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Area of Science:

  • Structural Biology
  • Biophysical Chemistry
  • Nuclear Magnetic Resonance (NMR) Spectroscopy

Background:

  • Solid-state NMR spectroscopy enables atomic-resolution studies of biomacromolecules.
  • Determining protein structures with solid-state NMR is hindered by limited long-range distance restraints.
  • Conventional methods struggle with biomacromolecules that are difficult to analyze structurally.

Purpose of the Study:

  • To develop a novel method for rapid determination of global protein fold in the solid phase.
  • To overcome the bottleneck of limited distance restraints in solid-state NMR structure elucidation.
  • To enable structural studies of challenging biomacromolecules using nuclear paramagnetic relaxation enhancements (PREs).

Main Methods:

  • Utilized nuclear paramagnetic relaxation enhancements (PREs) for distance measurements.
  • Employed analogues of the target protein with covalently attached paramagnetic tags (cysteine-EDTA-Cu(2+)).
  • Measured ~230 longitudinal backbone (15)N PREs in six mutants of Protein G's B1 domain.

Main Results:

  • Successfully determined the global protein fold in the solid phase without conventional internuclear distance restraints.
  • Obtained PREs corresponding to distances of approximately 10-20 Å.
  • The determined protein fold showed good agreement with the X-ray structure (backbone RMSD of 1.8 Å).

Conclusions:

  • Nuclear paramagnetic relaxation enhancements (PREs) provide a powerful tool for solid-state NMR structure determination.
  • This method effectively determines global protein fold for challenging biomacromolecules.
  • The approach offers a viable alternative to conventional distance restraints in structural studies.