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

What is Evolutionary History?02:35

What is Evolutionary History?

43.4K
Scientists record evolutionary history by analyzing fossil, morphological, and genetic data. The fossil record documents the history of life on Earth and provides evidence for evolution. However, both fossil and living organisms offer evidence that outlines Earth’s evolutionary history.
43.4K
¹H NMR: Long-Range Coupling01:27

¹H NMR: Long-Range Coupling

2.7K
The coupling interactions of nuclei across four or more bonds are usually weak, with J values less than 1 Hz. While these are usually not observed in spectra, the presence of multiple bonds along the coupling pathway can result in observable long-range coupling.
In alkenes, spin information is communicated via σ–π overlap, as seen in allylic (four-bond) and homoallylic (five-bond) couplings. These coupling interactions are stronger when the σ bond is parallel to the alkene...
2.7K
Protein and Protein Structure02:15

Protein and Protein Structure

87.5K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
87.5K
G-protein Coupled Receptors01:21

G-protein Coupled Receptors

132.0K
G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.
132.0K
NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

3.2K
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...
3.2K
Resonance and Hybrid Structures02:16

Resonance and Hybrid Structures

26.3K
According to the theory of resonance, if two or more Lewis structures with the same arrangement of atoms can be written for a molecule, ion, or radical, the actual distribution of electrons is an average of that shown by the various Lewis structures.
Resonance Structures and Resonance Hybrids
The Lewis structure of a nitrite anion (NO2−) may actually be drawn in two different ways, distinguished by the locations of the N–O and N=O bonds.
26.3K

You might also read

Related Articles

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

Sort by
Same author

High-throughput machine learning-aided antibody discovery for cell surface antigens.

Cell systems·2026
Same author

In silico discovery of nanobody binders to a G-protein coupled receptor using AlphaFold-Multimer.

Nature communications·2026
Same author

Determinants of metal import and specificity in a bacterial transporter.

bioRxiv : the preprint server for biology·2026
Same author

The 2025 Westlake Autumn Symposium for Al Proteomics and Virtual Cell.

Genomics, proteomics & bioinformatics·2026
Same author

Machine learning enables efficient and effective affinity maturation of nanobodies.

bioRxiv : the preprint server for biology·2026
Same author

Machine learning reveals hidden dimensions of functional similarity in proteins.

Proceedings of the National Academy of Sciences of the United States of America·2026

Related Experiment Video

Updated: Jan 31, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

10.1K

A Hybrid Approach for Protein Structure Determination Combining Sparse NMR with Evolutionary Coupling Sequence Data.

Yuanpeng Janet Huang1, Kelly P Brock2, Chris Sander3,2

  • 1Center for Advanced Biotechnology and Medicine, Department of Molecular Biology and Biochemistry, Rutgers, The State University of New Jersey, Piscataway, NJ, USA.

Advances in Experimental Medicine and Biology
|January 9, 2019
PubMed
Summary

A new hybrid EC-NMR method models larger protein structures using sparse NMR and evolutionary couplings (ECs). This approach enhances accuracy for larger proteins and speeds up smaller protein structure determination.

Keywords:
AutoStructure/ASDPAutomated NMR data analysisEvolutionary couplingsHybrid methodsMaximum entropyMultiple sequence alignmentProtein NMR spectroscopyProtein families

More Related Videos

Informatic Analysis of Sequence Data from Batch Yeast 2-Hybrid Screens
09:14

Informatic Analysis of Sequence Data from Batch Yeast 2-Hybrid Screens

Published on: June 28, 2018

7.5K
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

2.8K

Related Experiment Videos

Last Updated: Jan 31, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

10.1K
Informatic Analysis of Sequence Data from Batch Yeast 2-Hybrid Screens
09:14

Informatic Analysis of Sequence Data from Batch Yeast 2-Hybrid Screens

Published on: June 28, 2018

7.5K
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

2.8K

Area of Science:

  • Biophysics
  • Structural Biology
  • Computational Biology

Background:

  • Solution Nuclear Magnetic Resonance (NMR) spectroscopy is routine for small protein structures (<15 kDa).
  • Determining structures of larger proteins (>15 kDa) using NMR remains challenging.
  • Sequence co-variation data (evolutionary couplings, ECs) from protein families offers complementary structural information.

Purpose of the Study:

  • To introduce and validate a hybrid EC-NMR method for protein structure determination.
  • To assess the accuracy and efficiency of EC-NMR for proteins of varying sizes.
  • To explore the potential of EC-NMR for identifying alternative protein conformational states.

Main Methods:

  • Combining sparse NMR data from larger proteins with evolutionary couplings (ECs) derived from multiple sequence alignments.
  • Utilizing backbone NMR data for smaller proteins in conjunction with ECs.
  • Comparing EC-NMR derived structures with reference structures and full NMR assignment methods.

Main Results:

  • The EC-NMR method accurately models larger proteins (15-60 kDa).
  • It enables more rapid structure determination for smaller proteins (5-15 kDa) using only backbone NMR data.
  • EC-NMR structures achieve accuracy comparable to traditional full NMR assignments.
  • The method shows potential for identifying alternative protein states by analyzing EC-NMR consistency.

Conclusions:

  • The hybrid EC-NMR approach significantly advances protein structure determination, particularly for larger and challenging targets.
  • This method offers a powerful tool for both accurate modeling and rapid structural analysis.
  • EC-NMR holds promise for uncovering dynamic aspects of protein structure, including allosteric and excited states.