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

Protein Networks02:26

Protein Networks

4.7K
An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
4.7K
Protein-protein Interfaces02:04

Protein-protein Interfaces

15.0K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
15.0K
Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

2.8K
Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
2.8K

You might also read

Related Articles

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

Sort by
Same author

Inherent MS-cleavability of diazirine photo-cross-links enables residue-level structural analysis.

Nature communications·2026
Same author

Supramolecular Modulation of Photoinduced Charge Transfer: Tuning Between Tunneling and Incoherent Hopping.

Angewandte Chemie (International ed. in English)·2026
Same author

Mesenchymal stem cell-derived exosomes promote scalp rejuvenation through type XVII collagen regulation via the miR-21-5p/DKK2/Wnt pathway.

Frontiers in cell and developmental biology·2026
Same author

Dynamic Interfacial Evolution and Miscibility of CO<sub>2</sub>-Alkane Systems: The Role of Chain Length.

Langmuir : the ACS journal of surfaces and colloids·2026
Same author

Unveiling the Dynamic Ionic Interactions at the Single-Molecule Resolution.

Journal of the American Chemical Society·2026
Same author

The Impact of Real-Time Data Analytics on Infection Prevention and Control Practices in Ophthalmology: A Nursing Perspective on Patient Outcomes and Cost-Effectiveness.

Nursing & health sciences·2026

Related Experiment Video

Updated: Apr 14, 2026

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy NMR and Microscale Thermophoresis MST
10:28

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy NMR and Microscale Thermophoresis MST

Published on: November 2, 2018

12.8K

Transient protein-protein interactions visualized by solution NMR.

Zhu Liu1, Zhou Gong2, Xu Dong2

  • 1CAS Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic Molecular Physics, Wuhan Institute of Physics and Mathematics of the Chinese Academy of Sciences, Wuhan, Hubei Province 430071, China; Department of Pharmacology, Zhejiang University School of Medicine, Hangzhou, Zhejiang Province 310028, China; Institute of Neuroscience, Zhejiang University School of Medicine, Hangzhou, Zhejiang Province 310028, China.

Biochimica Et Biophysica Acta
|April 22, 2015
PubMed
Summary
This summary is machine-generated.

Nuclear Magnetic Resonance (NMR) techniques visualize transient protein-protein interactions at atomic resolution. Paramagnetic NMR, especially PRE, models ultraweak complexes and provides long-range restraints for larger protein interactions.

Keywords:
Chemical shift perturbationEnsemble averagingFleeting interactionNuclear magnetic resonanceParamagnetic relaxation enhancementProtein–protein interaction

More Related Videos

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
09:25

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Published on: November 1, 2024

3.0K
Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance
10:07

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance

Published on: August 26, 2025

711

Related Experiment Videos

Last Updated: Apr 14, 2026

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy NMR and Microscale Thermophoresis MST
10:28

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy NMR and Microscale Thermophoresis MST

Published on: November 2, 2018

12.8K
Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
09:25

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Published on: November 1, 2024

3.0K
Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance
10:07

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance

Published on: August 26, 2025

711

Area of Science:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • Protein-protein interactions are crucial for cellular functions.
  • Transient interactions, with dissociation constants (KD) in the μM-mM range, are vital for cell signaling.
  • Understanding these dynamic interactions is key to deciphering cellular mechanisms.

Purpose of the Study:

  • To review the application of solution Nuclear Magnetic Resonance (NMR) techniques for studying transient protein-protein interactions.
  • To highlight the capabilities of diamagnetic and paramagnetic NMR, including paramagnetic relaxation enhancement (PRE), in characterizing protein complexes.
  • To discuss the extraction of structural and dynamic information from NMR data, including encounter complexes and intrinsically disordered proteins.

Main Methods:

  • Solution NMR spectroscopy, including diamagnetic and paramagnetic approaches.
  • Paramagnetic relaxation enhancement (PRE) for long-range distance restraints in large complexes.
  • Integration of NMR with other biophysical techniques, such as single-molecule methods.

Main Results:

  • NMR provides atomic-resolution insights into transient protein-protein interactions.
  • Diamagnetic NMR characterizes complexes with KD up to several mM.
  • Paramagnetic NMR (PRE) models ultraweak complexes and aids in structural determination of large protein assemblies.
  • NMR data can reveal dynamic aspects like encounter complexes and coupled binding/folding.

Conclusions:

  • NMR is a powerful tool for visualizing and characterizing transient protein-protein interactions at atomic resolution.
  • Paramagnetic NMR (PRE) extends the reach of NMR to ultraweak and large complexes.
  • Future integration with single-molecule techniques will enhance the interpretation of NMR data for dynamic interactions.
  • In-cell NMR studies are anticipated to reveal differences in interaction dynamics compared to solution studies.