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

¹H NMR: Complex Splitting01:13

¹H NMR: Complex Splitting

1.7K
A proton M that is coupled to a proton X results in doublet signals for M. However, NMR-active nuclei can be simultaneously coupled to more than one nonequivalent nucleus. When M is coupled to a second proton A, such as in styrene oxide, each peak in the doublet is split into another doublet.
Splitting diagrams or splitting tree diagrams are routinely used to depict such complex couplings. While drawing splitting diagrams, the splitting with the larger coupling constant is usually applied...
1.7K
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

992
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...
992
Protein Organization01:24

Protein Organization

7.2K
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
7.2K
NMR and Mass Spectroscopy of Carboxylic Acids01:30

NMR and Mass Spectroscopy of Carboxylic Acids

3.8K
In ¹H NMR spectroscopy, acidic protons (–COOH) of carboxylic acids are highly deshielded and absorb far downfield, at around 9–12 ppm. The chemical shift value depends on the concentration and solvent used.
While α protons of carboxylic acids absorb at 2–2.5 ppm, β protons absorb further upfield.
Carboxylic acids are easily identified by dissolving them in deuterium oxide, which results in a rapid exchange of the acidic protons with deuterium. This leads to the...
3.8K
Double Resonance Techniques: Overview01:12

Double Resonance Techniques: Overview

870
Double resonance techniques in Nuclear Magnetic Resonance (NMR) spectroscopy involve the simultaneous application of two different frequencies or radiofrequency pulses to manipulate and observe two distinct nuclear spins. One important application of double resonance is spin decoupling, which selectively suppresses coupling with one type of nucleus while observing the NMR signal from another nucleus, simplifying the spectrum and enhancing resolution.
Spin decoupling is usually achieved by...
870
2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

801
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...
801

You might also read

Related Articles

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

Sort by
Same author

PEP-EDIT: a web server for the 3D generation and interactive editing of complex peptides.

Nucleic acids research·2026
Same author

Moving NMR infrastructures to remote access capabilities.

Progress in nuclear magnetic resonance spectroscopy·2026
Same author

Impact of shared facilities in advancing solid-state NMR research: 2025 edition.

Solid state nuclear magnetic resonance·2025
Same author

Simulated Solute Tempering 2: An Efficient and Practical Approach to Protein Conformational Sampling and Binding Events.

Journal of chemical theory and computation·2025
Same author

Robust Conformational Space Exploration of Cyclic Peptides by Combining Different MD Protocols and Force Fields.

Journal of chemical theory and computation·2025
Same author

Author Correction: Identification of new ClpC1-NTD binders for Mycobacterium tuberculosis drug development.

Scientific reports·2025
Same journal

pyTRACTnmr: an open source python package for analyzing [<sup>15</sup>N, <sup>1</sup>H]-TRACT experiments.

Journal of biomolecular NMR·2026
Same journal

RelCalc: symbolic evaluation of BWR theory relaxation rates in python, applications to TROSY effects in AX[Formula: see text] spin systems.

Journal of biomolecular NMR·2026
Same journal

Solution NMR study of the titin I-band IgI domain I82 shows unusual conformational dynamics.

Journal of biomolecular NMR·2026
Same journal

Methyl-specific NMR of therapeutic antibodies: cost-effective isotopic labeling strategies in CHO cells for high-resolution structural characterization.

Journal of biomolecular NMR·2026
Same journal

AMIGO - Guided assignment of <sup>13</sup>C-methyl labelled proteins.

Journal of biomolecular NMR·2026
Same journal

Super-Resolution solid-state NMR Spectroscopy.

Journal of biomolecular NMR·2026
See all related articles

Related Experiment Video

Updated: Apr 29, 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

9.3K

Robust structure-based resonance assignment for functional protein studies by NMR.

Dirk Stratmann1, Eric Guittet, Carine van Heijenoort

  • 1NMR, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands.

Journal of Biomolecular NMR
|December 22, 2009
PubMed
Summary
This summary is machine-generated.

NOEnet automates protein backbone assignment using structure-based nuclear magnetic resonance (NMR) data. This robust method provides accurate assignments, even with sparse data, enabling functional studies like protein complex modeling.

More Related Videos

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
12:47

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

17.7K
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

16.8K

Related Experiment Videos

Last Updated: Apr 29, 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

9.3K
Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
12:47

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

17.7K
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

16.8K

Area of Science:

  • Structural biology
  • Biophysics
  • Biochemistry

Background:

  • High-throughput protein nuclear magnetic resonance (NMR) studies require automated backbone assignment.
  • Structure-based assignment methods are emerging, utilizing NMR data beyond traditional J-coupling.

Purpose of the Study:

  • To present NOEnet, a robust structure-based approach for automated protein backbone assignment.
  • To demonstrate NOEnet's accuracy and utility in functional protein studies.

Main Methods:

  • Utilizes H(N)-H(N) NOE networks, (1)H-(15)N residual dipolar couplings, and chemical shifts.
  • Employs a complete search algorithm (NOEnet) robust against assignment errors and sparse data.
  • Combines NOEnet with limited J-coupling sequential connectivities for high-precision assignments.

Main Results:

  • NOEnet provides an optimal assignment ensemble with near 100% accuracy, even with sparse NMR data.
  • Low-precision assignment ensembles from NOEnet are sufficient for functional studies, including protein complex modeling.
  • Integration with J-coupling data enhances assignment precision.

Conclusions:

  • NOEnet offers a robust and accurate solution for automated protein backbone assignment in NMR studies.
  • The method facilitates functional analyses of proteins and protein complexes.
  • NOEnet is a valuable tool for structural biology and biophysics research.