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Related Concept Videos

NMR Spectrometers: Radiofrequency Pulses and Pulse Sequences01:17

NMR Spectrometers: Radiofrequency Pulses and Pulse Sequences

A pulse is a short burst of radio waves distributed over a range of frequencies that simultaneously excites all the nuclei in the sample. Upon passing a radio frequency pulse along the x-axis, the nuclei absorb energy corresponding to their Larmor frequencies and achieve resonance. This shifts the net magnetization vector from the z-axis toward the transverse plane. This angle of rotation of the magnetization vector, or the flip angle, is proportional to the duration and intensity of the pulse.
2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

Homonuclear correlation spectroscopy (COSY) is a powerful technique used in Nuclear Magnetic Resonance (NMR) spectroscopy to study the correlations between nuclei of the same type within a molecule. It provides information about scalar couplings between adjacent nuclei, which helps determine connectivity and structural information. There are several COSY variants, each with its unique strengths and experimental parameters.
COSY90 is the standard two-dimensional (2D) COSY experiment that...
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...
2D NMR: Homonuclear Correlation Spectroscopy (COSY)01:06

2D NMR: Homonuclear Correlation Spectroscopy (COSY)

Homonuclear correlation spectroscopy, or COSY, is a 2-dimensional NMR technique that provides information about coupled protons. Typically, the geminal and vicinal coupling are observed. For example, consider the COSY spectrum of ethyl acetate, where its 1D proton NMR spectrum is plotted along the vertical and horizontal axes with their corresponding chemical shift scale. Three spots on the diagonal corresponding to the three peaks in the 1D proton spectrum are called diagonal peaks. The COSY...
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.
NMR Spectrometers: Overview01:20

NMR Spectrometers: Overview

NMR spectrometers consist of a strong magnet, a radiofrequency transmitter, and a detector attached to a computer console for recording spectra of samples containing NMR-active nuclei. In first-generation NMR instruments called continuous-wave spectrometers, the resonance frequencies of the nuclei are determined by frequency-sweep or field-sweep methods. The magnetic field strength is fixed and the rf signal is swept in the former, while the radiofrequency signal is fixed and the magnetic field...

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Related Experiment Video

Updated: May 8, 2026

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale
08:09

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale

Published on: April 19, 2021

Motion-adapted pulse sequences for oriented sample (OS) solid-state NMR of biopolymers.

George J Lu1, Stanley J Opella

  • 1Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California 92093-0307, USA.

The Journal of Chemical Physics
|September 7, 2013
PubMed
Summary

Solid-state NMR uses motion-adapted pulse sequences to improve spectral quality for biopolymers like membrane proteins. This technique reduces spectral line widths by accounting for molecular dynamics during NMR radiofrequency irradiation.

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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

Related Experiment Videos

Last Updated: May 8, 2026

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale
08:09

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale

Published on: April 19, 2021

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

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

Published on: September 17, 2017

Area of Science:

  • Solid-state Nuclear Magnetic Resonance (NMR) spectroscopy.
  • Biophysical chemistry.
  • Structural biology.

Background:

  • Solid-state NMR is crucial for studying biopolymer structure and dynamics, especially membrane proteins in physiological conditions.
  • Molecular motions significantly influence Nuclear Magnetic Resonance (NMR) radiofrequency irradiation effects on nuclear spins.
  • Previous work demonstrated reduced spectral line widths using MSHOT-Pi4 for membrane proteins with rapid rotational diffusion.

Purpose of the Study:

  • To experimentally and analytically demonstrate how Hamiltonian terms are affected by sample motions.
  • To explain the "motion adapted" property of the MSHOT-Pi4 pulse sequence through critical π/2 Z-rotational symmetry.
  • To generalize this approach for designing superior decoupling sequences for molecular motions in NMR.

Main Methods:

  • Experimental validation of the MSHOT-Pi4 pulse sequence's effectiveness.
  • Analytical description of Hamiltonian term susceptibility to molecular motion.
  • Design and generalization of motion-adapted pulse sequences for Nuclear Magnetic Resonance (NMR).

Main Results:

  • Demonstrated that specific Hamiltonian terms are susceptible to sample motions.
  • Identified critical π/2 Z-rotational symmetry as key to the "motion adapted" property.
  • Developed the "Motion-adapted SAMPI4" pulse sequence and a generalized approach for superior decoupling sequences.

Conclusions:

  • The "motion adapted" property arises from removing motion-susceptible Hamiltonian terms via Z-rotational symmetry.
  • This approach enables the design of advanced decoupling sequences that outperform conventional methods in the presence of molecular motion.
  • The developed methodology is applicable to both stationary and magic angle spinning solid-state NMR experiments.