Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

1.1K
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...
1.1K
Spin–Spin Coupling Constant: Overview01:08

Spin–Spin Coupling Constant: Overview

1.1K
In bromoethane, the three methyl protons are coupled to the two methylene protons that are three bonds away. In accordance with the n+1 rule, the signal from the methyl protons is split into three peaks with 1:2:1 relative intensities. The methylene protons appear as a quartet, with the relative intensities of 1:3:3:1.
Qualitatively, any spin plus-half nucleus polarizes the spins of its electrons to the minus-half state. Consequently, the paired electron in the hydrogen–carbon bond must...
1.1K
Atomic Nuclei: Nuclear Spin State Population Distribution01:14

Atomic Nuclei: Nuclear Spin State Population Distribution

1.4K
Near absolute zero temperatures, in the presence of a magnetic field, the majority of nuclei prefer the lower energy spin-up state to the higher energy spin-down state. As temperatures increase, the energy from thermal collisions distributes the spins more equally between the two states. The Boltzmann distribution equation gives the ratio of the number of spins predicted in the spin −½ (N−) and spin +½ (N+) states.
1.4K
Atomic Nuclei: Types of Nuclear Relaxation01:28

Atomic Nuclei: Types of Nuclear Relaxation

436
Nuclear relaxation restores the equilibrium population imbalance and can occur via spin–lattice or spin–spin mechanisms, which are first-order exponential decay processes.
In spin–lattice or longitudinal relaxation, the excited spins exchange energy with the surrounding lattice as they return to the lower energy level. Among several mechanisms that contribute to spin–lattice relaxation, magnetic dipolar interactions are significant. Here, the excited nucleus transfers...
436
Atomic Nuclei: Nuclear Spin State Overview01:03

Atomic Nuclei: Nuclear Spin State Overview

1.2K
NMR-active nuclei have energy levels called 'spin states' that are associated with the orientations of their nuclear magnetic moments. In the absence of a magnetic field, the nuclear magnetic moments are randomly oriented, and the spin states are degenerate. When an external magnetic field is applied, the spin states have only 2 + 1 orientations available to them. A proton with = ½ has two available orientations. Similarly, for a quadrupolar nucleus with a nuclear spin value of...
1.2K
Atomic Nuclei: Nuclear Relaxation Processes01:23

Atomic Nuclei: Nuclear Relaxation Processes

758
In the absence of an external magnetic field, nuclear spin states are degenerate and randomly oriented. When a magnetic field is applied, the spins begin to precess and orient themselves along (lower energy) or against (higher energy) the direction of the field. At equilibrium, a slight excess population of spins exists in the lower energy state. Because the direction of the magnetic field is fixed as the z-axis,  the precessing magnetic moments are randomly oriented around the z-axis.
758

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Molecular basis for depsipeptide HDAC inhibitor combinatorial biosynthesis.

Nature communications·2026
Same author

Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes.

Nature chemistry·2026
Same author

Structural Insights into Native Intact <i>Mycobacterium abscessus</i> by Conventional and Ultrahigh-field solid-state NMR at 1.2 GHz.

bioRxiv : the preprint server for biology·2026
Same author

Real-time monitoring of glycocarrier formation unravels cryptic details in glycosyl transfer.

RSC chemical biology·2026
Same author

Impact of shared facilities in advancing solid-state NMR research: 2025 edition.

Solid state nuclear magnetic resonance·2025
Same author

Molecular characterisation of the acyltransferase-acyl carrier protein interface in a fungal highly reducing polyketide synthase.

RSC chemical biology·2025

Related Experiment Video

Updated: Oct 8, 2025

Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels
11:19

Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels

Published on: July 4, 2016

10.7K

Dipolar Order Parameters in Large Systems With Fast Spinning.

W Trent Franks1,2, Ben P Tatman1,2, Jonah Trenouth2

  • 1Department of Physics, University of Warwick, Coventry, United Kingdom.

Frontiers in Molecular Biosciences
|December 27, 2021
PubMed
Summary

This study introduces a new method for measuring molecular motion using dipolar order parameters. These measurements help understand protein dynamics within large complexes.

Keywords:
dynamicsfast MAS NMRorder parameterproton detectionrecouplingsymmetry

More Related Videos

Dissolution Dynamic Nuclear Polarization Instrumentation for Real-time Enzymatic Reaction Rate Measurements by NMR
10:54

Dissolution Dynamic Nuclear Polarization Instrumentation for Real-time Enzymatic Reaction Rate Measurements by NMR

Published on: February 23, 2016

10.8K
Measuring the Spin-Lattice Relaxation Magnetic Field Dependence of Hyperpolarized [1-13C]pyruvate
11:57

Measuring the Spin-Lattice Relaxation Magnetic Field Dependence of Hyperpolarized [1-13C]pyruvate

Published on: September 13, 2019

6.7K

Related Experiment Videos

Last Updated: Oct 8, 2025

Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels
11:19

Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels

Published on: July 4, 2016

10.7K
Dissolution Dynamic Nuclear Polarization Instrumentation for Real-time Enzymatic Reaction Rate Measurements by NMR
10:54

Dissolution Dynamic Nuclear Polarization Instrumentation for Real-time Enzymatic Reaction Rate Measurements by NMR

Published on: February 23, 2016

10.8K
Measuring the Spin-Lattice Relaxation Magnetic Field Dependence of Hyperpolarized [1-13C]pyruvate
11:57

Measuring the Spin-Lattice Relaxation Magnetic Field Dependence of Hyperpolarized [1-13C]pyruvate

Published on: September 13, 2019

6.7K

Area of Science:

  • Biophysics
  • Structural Biology
  • Nuclear Magnetic Resonance (NMR) Spectroscopy

Background:

  • Order parameters are crucial for quantifying molecular motion amplitudes.
  • Measuring these parameters, especially in complex biological systems, presents significant challenges.
  • Nuclear Magnetic Resonance (NMR) is a powerful technique for probing molecular dynamics.

Purpose of the Study:

  • To develop and validate a novel method for measuring dipolar order parameters.
  • To quantify site-specific molecular motions in proteins using fast magic angle spinning NMR.
  • To investigate protein dynamics within large, aggregated complexes.

Main Methods:

  • Utilized symmetry-based recoupling methods under fast magic angle spinning (60 kHz).
  • Employed a variable flip angle compound inversion pulse to recouple heteronuclear dipole-dipole couplings.
  • Measured site-specific 15N-1H order parameters in microcrystalline protein and protein-antibody complexes.

Main Results:

  • Successfully measured site-specific 15N-1H order parameters across a temperature range.
  • Demonstrated the method's applicability to a protein within a large, precipitated antibody complex.
  • The order parameters indicated overall motion of the protein within the complex.

Conclusions:

  • The developed method accurately quantifies molecular motion amplitudes.
  • This technique is valuable for studying protein dynamics in complex biological assemblies.
  • The findings provide insights into the dynamic behavior of proteins in aggregated states.