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

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...

¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR

¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR

The axial and equatorial protons in cyclohexane can be distinguished by performing a variable-temperature NMR experiment. In this process, except for one proton, the remaining eleven protons are replaced by deuterium. The deuterium substitution avoids the possible peak splitting caused by the spin-spin coupling between the adjacent protons. The remaining proton flips between the axial and equatorial positions.

Interpreting ¹H NMR Signal Splitting: The (n + 1) Rule

Interpreting ¹H NMR Signal Splitting: The (n + 1) Rule

In the AX proton spin system, proton A can sense the two spin states of a coupled proton X, resulting in a doublet NMR signal with two peaks of equal (1:1) intensity. When proton A is coupled to two equivalent protons (AX2 spin system), the spin states of each X can be aligned with or against the external field, creating three possible scenarios. This results in a 1:2:1 triplet signal, where the central peak corresponds to the chemical shift of A and is twice as large or intense as the...

You might also read

Related Articles

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

Sort by

Same author

Structural and mutational insights define ERMA as the ER Mg<sup>2+</sup> ATPase and reservoir gatekeeper.

Science advances·2026

Same author

Dual engagement of Spike and ACE2 by annexin A5 contributes to pleiotropic SARS-CoV-2 inhibition.

Scientific reports·2026

Same author

Human pannexin mutations and their implications in erosive osteoarthritis.

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

Same author

Defining the interactome of the pancreas-specific SPCA2 isoform (SPCA2C) identifies unique links to store-operated Ca<sup>2+</sup> entry.

The FEBS journal·2025

Same author

Disrupting the network of co-evolving amino terminal domain residues relieves mitochondrial calcium uptake inhibition by MCUb.

Computational and structural biotechnology journal·2025

Same author

The apo LETM1 F-EF-hand adopts a closed conformation that underlies a multi-modal sensory role in mitochondria.

FEBS letters·2025

Search research articles

Related Experiment Video

Updated: Sep 13, 2025

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Protocol for deriving distance restraints from AlphaFold for use in solution NMR structure determination.

Qi-Tong Lin¹, Peter B Stathopulos¹

¹Department of Physiology and Pharmacology, Schulich School of Medicine and Dentistry, University of Western Ontario, London, Ontario N6A5C1, Canada.

|July 30, 2025

Summary

Artificial intelligence (AI) aids structural biology by reliably deriving distance restraints from AlphaFold predictions. This automates nuclear Overhauser effect (NOE) assignment for faster, more accurate solution NMR structure determination.

Keywords:

NMR structural biology

More Related Videos

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

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

Published on: December 16, 2013

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Published on: October 2, 2017

Related Experiment Videos

Last Updated: Sep 13, 2025

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

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

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

Published on: December 16, 2013

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Published on: October 2, 2017

Area of Science:

Structural biology
Computational biology
Biophysics

Background:

Artificial intelligence (AI) is transforming structural biology.
Reliable application of AI tools is crucial for scientific advancement.
Nuclear Overhauser effect (NOE) assignment is key in solution NMR structure determination.

Purpose of the Study:

To present a reliable method for deriving distance restraints from AlphaFold structure predictions.
To facilitate automated nuclear Overhauser effect (NOE) assignment in solution NMR.
To enhance the accuracy and efficiency of protein structure determination.

Main Methods:

Selection of reliable AlphaFold structure predictions.
Determination of interatomic distances from predicted structures.
Generation of high-confidence distance restraints for NMR analysis.

Main Results:

Successful derivation of distance restraints from AlphaFold models.
Demonstrated utility in automating NOE assignment.
Improved accuracy and reduced ambiguity in structure determination.

Conclusions:

The presented protocol expedites solution NMR structure determination.
This approach enhances the elucidation of elusive protein structures.
It provides a method for validating AI-driven structural predictions.