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-protein Interfaces02:04

Protein-protein Interfaces

12.7K
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...
12.7K
NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

1.6K
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...
1.6K
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

3.8K
3.8K
2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

275
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...
275
Protein Networks02:26

Protein Networks

4.1K
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,...
4.1K
NMR Spectroscopy Of Amines01:19

NMR Spectroscopy Of Amines

9.3K
In proton NMR spectroscopy, primary amines and secondary amines showcase their N–H protons as a broad signal in the chemical shift range between δ 0.5 and 5 ppm. The exact position in this range depends on several factors, including sample concentration, hydrogen bonding, and the type of solvent used. Since amine protons undergo fast proton exchange in solution, the protons are labile and therefore do not participate in any splitting with adjacent protons. Thus, the observed peak is...
9.3K

You might also read

Related Articles

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

Sort by
Same author

Slow Dynamics Orchestrate Communication Between Binding Sites in the Condensation Domain of a Non-ribosomal Peptide Synthetase.

Journal of molecular biology·2025
Same author

NMR chemical shift assignment of the IMLV methyl groups of a di-domain of the Tomaymycin non-ribosomal peptide synthetase.

Biomolecular NMR assignments·2025
Same author

PIN1-SUMO2/3 motif suppresses excessive RNF168 chromatin accumulation and ubiquitin signaling to promote IR resistance.

Nature communications·2025
Same author

Long-range conformational changes in the nucleotide-bound states of the DEAD-box helicase Vasa.

Biophysical journal·2024
Same author

The specificity of intermodular recognition in a prototypical nonribosomal peptide synthetase depends on an adaptor domain.

Science advances·2024
Same author

Phosphopeptide binding to the N-SH2 domain of tyrosine phosphatase SHP2 correlates with the unzipping of its central β-sheet.

Computational and structural biotechnology journal·2024

Related Experiment Video

Updated: Aug 29, 2025

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

15.5K

Nucleic acid-protein interfaces studied by MAS solid-state NMR spectroscopy.

Philipp Innig Aguion1, Alexander Marchanka1,2, Teresa Carlomagno3

  • 1Institute for Organic Chemistry and Centre of Biomolecular Drug Research (BMWZ), Leibniz University Hannover, Schneiderberg 38, 30167 Hannover, Germany.

Journal of Structural Biology: X
|September 12, 2022
PubMed
Summary
This summary is machine-generated.

Solid-state NMR (ssNMR) now enables structural studies of challenging RNA-protein complexes. This review covers ssNMR methods and the first complex structure determined using these techniques.

Keywords:
Intermolecular interfacesNucleic acid-protein complexesssNMR

More Related Videos

Author Spotlight: Unveiling the Structural and Dynamic Aspects of Glycan Molecular Recognition
07:40

Author Spotlight: Unveiling the Structural and Dynamic Aspects of Glycan Molecular Recognition

Published on: May 17, 2024

1.4K
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

12.2K

Related Experiment Videos

Last Updated: Aug 29, 2025

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

15.5K
Author Spotlight: Unveiling the Structural and Dynamic Aspects of Glycan Molecular Recognition
07:40

Author Spotlight: Unveiling the Structural and Dynamic Aspects of Glycan Molecular Recognition

Published on: May 17, 2024

1.4K
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

12.2K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Solid-state NMR (ssNMR) is effective for large protein assemblies but limited for nucleic acid-protein complexes due to signal overlap.
  • Recent advancements have enabled RNA structure determination by ssNMR, paving the way for complex studies.

Purpose of the Study:

  • To review ssNMR methodologies for investigating nucleic acid-protein interfaces.
  • To highlight the first structure determination of an RNA-protein complex using ssNMR.

Main Methods:

  • Review of ssNMR techniques including chemical shift/peak intensity perturbations.
  • Application of direct distance measurements and paramagnetic effects.
  • Utilizing ssNMR-derived intermolecular restraints for structure determination.

Main Results:

  • Established ssNMR methodologies for analyzing nucleic acid-protein interactions.
  • Demonstrated the feasibility of determining RNA-protein complex structures via ssNMR.
  • Presented the first ssNMR-based structure of an RNA-protein complex.

Conclusions:

  • ssNMR is a powerful tool for elucidating nucleic acid-protein complex structures.
  • The reviewed methods provide new avenues for structural biology research.
  • This work establishes a foundation for future ssNMR studies of biomolecular complexes.