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

You might also read

Related Articles

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

Sort by
Same author

Optimizing ensemble NV<sup>-</sup> spin properties of fluorescent diamond microparticles by systematic low pressure high temperature annealing.

Frontiers in quantum science and technology·2026
Same author

Radical <i>S</i>-Adenosyl-l-Methionine Oxygenase DarE Forms Ether Bond via a Partially Delocalized Tryptophan C<sub>β</sub> Radical.

Journal of the American Chemical Society·2026
Same author

Electronic Spin Relaxation and Clustering in High Pressure High Temperature Synthesized Microcrystalline Diamond Particles with Reduced Nitrogen Content.

The journal of physical chemistry. C, Nanomaterials and interfaces·2025
Same author

Room-Temperature Pulsed Dynamic Nuclear Polarization at 7 T.

The journal of physical chemistry letters·2025
Same author

Assembly of a Heterobimetallic Fe/Mn Cofactor in the <i>para</i>-Aminobenzoate Synthase Chlamydia Protein Associating with Death Domains (CADD) Initiates Long-Range Radical Hole-Hopping.

Biochemistry·2024
Same author

A roadmap to advance exposomics through federation of data.

Exposome·2024

Related Experiment Video

Updated: Mar 31, 2026

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

11.2K

Peptide-Membrane Interactions by Spin-Labeling EPR.

Tatyana I Smirnova1, Alex I Smirnov1

  • 1Department of Chemistry, North Carolina State University, Raleigh, North Carolina, USA.

Methods in Enzymology
|October 20, 2015
PubMed
Summary

Site-directed spin labeling (SDSL) coupled with electron paramagnetic resonance (EPR) spectroscopy is a powerful tool for studying peptide-membrane interactions. This method quantifies peptide binding, topology, and aggregation with minimal disruption to the peptide.

Keywords:
Accessibility EPR experimentsBinding isothermsMembrane mimeticsPeptide aggregationPeptide binding

More Related Videos

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
07:24

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

2.4K
Purification and Reconstitution of TRPV1 for Spectroscopic Analysis
11:53

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis

Published on: July 3, 2018

8.5K

Related Experiment Videos

Last Updated: Mar 31, 2026

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

11.2K
Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
07:24

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

2.4K
Purification and Reconstitution of TRPV1 for Spectroscopic Analysis
11:53

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis

Published on: July 3, 2018

8.5K

Area of Science:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • Site-directed spin labeling (SDSL) coupled with electron paramagnetic resonance (EPR) spectroscopy is increasingly utilized in protein and peptide science.
  • Advancements in labeling strategies and EPR instrumentation have driven the popularity and applicability of this technique.
  • SDSL introduces a paramagnetic probe at specific peptide positions, minimally affecting peptide structure and energetics of membrane interactions.

Purpose of the Study:

  • To describe fundamental approaches for employing SDSL EPR spectroscopy to investigate small peptide interactions with biological membranes and membrane mimetics.
  • To detail experimental methods for quantifying peptide-membrane binding affinity and determining the topology of bound peptides.
  • To outline strategies for characterizing peptide aggregation using SDSL EPR.

Main Methods:

  • Site-directed spin labeling (SDSL) to introduce paramagnetic probes at defined peptide locations.
  • Electron paramagnetic resonance (EPR) spectroscopy for analyzing labeled peptides.
  • Preparation of membrane mimetic systems and detailed sample preparation protocols.

Main Results:

  • Demonstration of SDSL EPR as a robust method for studying peptide-membrane interactions.
  • Establishment of experimental protocols for quantifying peptide binding and topology.
  • Characterization of peptide aggregation states within membrane environments.

Conclusions:

  • SDSL EPR spectroscopy provides a minimally disruptive yet powerful approach to study peptide-membrane interactions.
  • The described methods enable quantitative analysis of peptide binding, localization, and aggregation.
  • This technique is valuable for understanding peptide behavior in biological membrane contexts.