Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)

¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)

When proton-coupled carbon-13 spectra are simplified by a broadband proton decoupling technique, structural information about the coupled protons is lost. Distortionless enhancement by polarization transfer (DEPT) is a technique that provides information on the number of hydrogens attached to each carbon in a molecule. While the DEPT experiment utilizes complex pulse sequences, the pulse delay and flip angle are specifically manipulated. The resulting signals have different phases depending on...

¹³C NMR: ¹H–¹³C Decoupling

¹³C NMR: ¹H–¹³C Decoupling

The probability of having two carbon-13 atoms next to each other is negligible because of the low natural abundance of carbon-13. Consequently, peak splitting due to carbon-carbon spin-spin coupling is not observed in spectra. However, protons up to three sigma bonds away split the carbon signal according to the n+1 rule, resulting in complicated spectra.
A broadband decoupling technique is used to simplify these complex, sometimes overlapping, signals. Broadband decoupling relies on a...

You might also read

Related Articles

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

Sort by

Same author

Comment on "Effective spin Hamiltonians for the quantum-rotor tunneling problem in pulse EPR" [J. Chem. Phys. 163, 064104 (2025)].

The Journal of chemical physics·2026

Same author

Towards full optimisation of automated double electron-electron resonance spectroscopy.

Physical chemistry chemical physics : PCCP·2025

Same author

Design of facilitated dissociation enables timing of cytokine signalling.

Nature·2025

Same author

Recent advances in quantifying protein conformational ensembles with dipolar EPR spectroscopy.

Current opinion in structural biology·2025

Same author

Human contributions to global soundscapes are less predictable than the acoustic rhythms of wildlife.

Nature ecology & evolution·2025

Same author

Effects of land cover and protected areas on flying insect diversity.

Conservation biology : the journal of the Society for Conservation Biology·2024

Same journal

A Tubules-First Model for the Origin of Eukaryotic Membrane Traffic.

Annual review of biophysics·2026

Same journal

Seeking Biology's Physics Stories: Simplify, Simplify.

Annual review of biophysics·2026

Same journal

Pattern Formation Beyond Turing: Physical Principles of Mass-Conserving Reaction-Diffusion Systems.

Annual review of biophysics·2026

Same journal

Rigidity and Mechanical Response in Biological Structures.

Annual review of biophysics·2026

Same journal

Systems Biology of Aging, Metabolism, and Mitochondria.

Annual review of biophysics·2026

Same journal

Ligand Binding Dynamics of Ion Channels and GPCRs Using Single-Molecule Fluorescence.

Annual review of biophysics·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Jun 12, 2025

Analysis of SEC-SAXS data via EFA deconvolution and Scatter

Analysis of SEC-SAXS data via EFA deconvolution and Scatter

Published on: January 28, 2021

Protein Modeling with DEER Spectroscopy.

Maxx H Tessmer¹, Stefan Stoll¹

¹Department of Chemistry, University of Washington, Seattle, Washington, USA;

Annual Review of Biophysics

|December 17, 2024

Summary

This summary is machine-generated.

Double electron-electron resonance (DEER) and spin labeling reveal protein structures. This review details protein and spin label modeling methods for accurate distance measurements and conformational landscape analysis.

Keywords:

DEER EPR spectroscopy integrative modeling spin labeling

More Related Videos

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis

Published on: July 3, 2018

Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics

Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics

Published on: April 17, 2017

Related Experiment Videos

Last Updated: Jun 12, 2025

Analysis of SEC-SAXS data via EFA deconvolution and Scatter

Analysis of SEC-SAXS data via EFA deconvolution and Scatter

Published on: January 28, 2021

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis

Published on: July 3, 2018

Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics

Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics

Published on: April 17, 2017

Area of Science:

Biophysics
Structural Biology
Computational Biology

Background:

Double electron-electron resonance (DEER) with site-directed spin labeling is crucial for determining distance distributions between protein residues.
Accurate protein structure and conformational heterogeneity analysis relies on effective modeling of DEER data.

Purpose of the Study:

To review the application of DEER data in protein modeling.
To highlight the importance of spin label modeling for extracting precise structural information.
To discuss the potential of DEER for modeling conformational landscapes.

Main Methods:

Review of spin label modeling techniques for DEER data analysis.
Discussion of protein modeling strategies using DEER restraints.
Identification and analysis of common artifacts in DEER experiments.

Main Results:

Spin label modeling is essential for accurate distance measurements in proteins.
DEER data enables the modeling of protein structural ensembles and conformational landscapes.
Effective site selection and application of DEER restraints are critical for successful protein modeling.

Conclusions:

Protein modeling with DEER data is a powerful technique for investigating protein structure and dynamics.
The review provides insights into common applications and future outlooks for DEER in structural biology.