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

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...
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...
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...
Double Resonance Techniques: Overview01:12

Double Resonance Techniques: Overview

Double resonance techniques in Nuclear Magnetic Resonance (NMR) spectroscopy involve the simultaneous application of two different frequencies or radiofrequency pulses to manipulate and observe two distinct nuclear spins. One important application of double resonance is spin decoupling, which selectively suppresses coupling with one type of nucleus while observing the NMR signal from another nucleus, simplifying the spectrum and enhancing resolution.
Spin decoupling is usually achieved by...
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...
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...

You might also read

Related Articles

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

Sort by
Same author

Cardiopulmonary exercise testing-derived circulatory power predicts major adverse cardiac events in adults with repaired tetralogy of Fallot.

Annals of pediatric cardiology·2026
Same author

Advances and unmet needs in pharmacologic therapy for pediatric heart failure: Insights from the 2025 International Society for Heart and Lung Transplantation Guidelines.

Annals of pediatric cardiology·2026
Same author

Heart Transplant Outcomes in Chemotherapy-Induced vs. Non-Ischemic-Dilated Cardiomyopathy: Pediatric and Adult Recipients in the Ventricular Assist Device Era.

Reviews in cardiovascular medicine·2026
Same author

Pediatric Myocarditis: Challenges in Diagnosis and Treatment.

Paediatric drugs·2026
Same author

Predicting 1-Year Mortality After Pediatric Heart Transplantation Using Machine Learning: A Systematic Review and Meta-Analysis.

JACC. Advances·2025
Same author

Pediatric Heart Failure Pharmacotherapy: Transformative Insights for the Future.

Reviews in cardiovascular medicine·2025
Same journal

Donor-Acceptor Separation Augments Temperature Dependence of Kinetic Isotope Effects in NADH Model Hydride Transfer Reactions: Mimicking Enzyme versus Mutant Dynamics.

The journal of physical chemistry. B·2026
Same journal

Disordered Worm-Like Clusters in a Hexagonal Mesophase Former: Simulation and Thermodynamic Description.

The journal of physical chemistry. B·2026
Same journal

Comparative Biophysical Analysis of Healthy and Inflamed Intestinal Membrane Models Using Langmuir Monolayers.

The journal of physical chemistry. B·2026
Same journal

Phosphoserine Charge State Drives Ion Condensation and Spatial Polyamine Presentation in Multirepeat Silaffin.

The journal of physical chemistry. B·2026
Same journal

pH-Dependent Conformational Transition of the Glutamate-GABA Antiporter GadC Revealed by <sup>19</sup>F NMR.

The journal of physical chemistry. B·2026
Same journal

Hydrogen-Bond Network in Equimolar <i>N</i>-Methylacetamide-Water: Integrated Neutron Scattering, Molecular Dynamics, DFT-NBO-AIM, and Machine Learning Analysis.

The journal of physical chemistry. B·2026
See all related articles

Related Experiment Video

Updated: May 7, 2026

High-Temperature and High-Pressure In situ Magic Angle Spinning Nuclear Magnetic Resonance Spectroscopy
08:55

High-Temperature and High-Pressure In situ Magic Angle Spinning Nuclear Magnetic Resonance Spectroscopy

Published on: October 9, 2020

Experiments optimized for magic angle spinning and oriented sample solid-state NMR of proteins.

Bibhuti B Das1, Eugene C Lin, Stanley J Opella

  • 1University of California, San Diego , 9500 Gilman Drive, 0307 La Jolla, California 92093-0307, United States.

The Journal of Physical Chemistry. B
|September 19, 2013
PubMed
Summary
This summary is machine-generated.

New solid-state NMR techniques enhance polarization transfer efficiency for protein structure determination. These methods improve sensitivity, aiding in the structural analysis of membrane proteins under physiological conditions.

More Related Videos

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

Related Experiment Videos

Last Updated: May 7, 2026

High-Temperature and High-Pressure In situ Magic Angle Spinning Nuclear Magnetic Resonance Spectroscopy
08:55

High-Temperature and High-Pressure In situ Magic Angle Spinning Nuclear Magnetic Resonance Spectroscopy

Published on: October 9, 2020

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:

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

Background:

  • Solid-state NMR is a powerful technique for protein structure determination.
  • Advancements in sample preparation, experimental methods, and computational approaches are driving progress.
  • Current methods face challenges in coherence transfer efficiency, particularly for membrane proteins.

Purpose of the Study:

  • To improve the efficiency of polarization transfer in solid-state NMR experiments.
  • To develop enhanced techniques for structural analysis of membrane proteins.
  • To optimize experimental conditions for proteins in phospholipid bilayers.

Main Methods:

  • Utilized adiabatic demagnetization and remagnetization on stationary aligned samples.
  • Employed proton-assisted insensitive nuclei cross-polarization (icp) in magic angle spinning (MAS) samples.
  • Applied multidimensional correlation spectroscopy of low-gamma nuclei (15N and 13C).

Main Results:

  • Achieved significant sensitivity enhancements (40-100%) in cross-polarization efficiency.
  • Demonstrated improved polarization transfer using adiabatic cross-polarization techniques.
  • Showcased the applicability of these methods for membrane proteins in lipid bilayers.

Conclusions:

  • The developed solid-state NMR techniques substantially enhance polarization transfer efficiency.
  • These advancements facilitate more accurate and sensitive structural determination of proteins, especially membrane proteins.
  • The optimized methods are suitable for studying proteins under physiological conditions in phospholipid bilayers.