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

Applications Of NMR In Biology01:25

Applications Of NMR In Biology

4.3K
Nuclear magnetic resonance (NMR) spectroscopy is a very valuable analytical technique for researchers. It has been used for more than 50 years as an analytical tool. F. Bloch and E. Purcell formulated NMR in 1946 and won the 1952 Nobel Prize in Physics  for their work. Biological macromolecules such as proteins, nucleic acids, lipids, and organic molecules including pharmaceutical compounds, can be studied using this versatile tool that exploits the magnetic properties of certain nuclei.
4.3K
Other Nuclides: 31P, 19F, 15N NMR01:16

Other Nuclides: 31P, 19F, 15N NMR

663
Many organic, inorganic, and biological molecules contain spin-half nuclei such as nitrogen-15, fluorine-19, and phosphorus-31. As a result, NMR studies of these nuclei have found extensive applications in chemical and biological research.
While fluorine-19 and phosphorous-31 have high natural abundances (100%) and positive gyromagnetic ratios, nitrogen-15 has a low natural abundance and a negative gyromagnetic ratio. However, nitrogen-15 is still preferred over nitrogen-14 (which has a...
663
Nuclear Magnetic Resonance (NMR): Overview01:07

Nuclear Magnetic Resonance (NMR): Overview

6.3K
Nuclear magnetic resonance (NMR) is a phenomenon exhibited by certain nuclei that can absorb characteristic radio frequency radiation under certain conditions. NMR has been extensively applied in molecular spectroscopy and medical diagnostic imaging. In both these applications, the molecule or subject under study is placed in a magnetic field and irradiated with radio frequency energy.
NMR spectroscopy generates a spectrum where the characteristic absorption frequencies of the sample are...
6.3K
Atomic Nuclei: Magnetic Resonance01:05

Atomic Nuclei: Magnetic Resonance

1.0K
The number of nuclear spins aligned in the lower energy state is slightly greater than those in the higher energy state. In the presence of an external magnetic field, as the spins precess at the Larmor frequency, the excess population results in a net magnetization oriented along the z axis. When a pulse or a short burst of radio waves at the Larmor frequency is applied along the x axis, the coupling of frequencies causes resonance and flips the nuclear spins of the excess population from the...
1.0K
Two-Dimensional (2D) NMR: Overview01:12

Two-Dimensional (2D) NMR: Overview

1.3K
The 1D NMR spectrum of large and complex molecules like natural products has complicated splitting patterns and overlapping signals, which can be easily interpreted using 2-dimensional (2D) NMR. Unlike 1D NMR, 2D NMR has two frequency axes that provide the coupling information between the nucleus A and nucleus B in a molecule. The process from which 2D spectra are obtained has four steps.
The first step is the preparation period, during which nucleus A is excited with a radiofrequency pulse....
1.3K
NMR Spectrometers: Resolution and Error Correction01:14

NMR Spectrometers: Resolution and Error Correction

977
When magnetic nuclei in a sample achieve resonance and undergo relaxation, the signal detected in NMR is an approximately exponential free induction decay. Fourier transform of an exponential decay yields a Lorentzian peak in the frequency domain. Lorentzian peaks in an NMR spectrum are defined by their amplitude, full width at half maximum, and position, where the peak width is governed by the spin-spin relaxation time alone. In real experiments, however, the applied magnetic field is rendered...
977

You might also read

Related Articles

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

Sort by
Same author

Identification of a Shiga toxin A-derived peptide internalized into Gb3 receptor-bearing cells via interaction with the Shiga toxin B subunit.

FEBS letters·2026
Same author

Enzyme-Free Phosphorylation with Kinetic Gating in a De Novo Coiled-Coil System.

Journal of the American Chemical Society·2026
Same author

Conformational Quenching in an Engineered Lipocalin Protein Achieves High Affinity Binding to the Toxin Colchicine.

Angewandte Chemie (International ed. in English)·2025
Same author

The Paulinella chromatophore transit peptide part2 adopts a structural fold similar to the γ-glutamyl-cyclotransferase fold.

Plant physiology·2025
Same author

QKI ensures splicing fidelity during cardiogenesis by engaging the U6 tri-snRNP to activate splicing at weak 5' splice sites.

bioRxiv : the preprint server for biology·2025
Same author

Deciphering the RNA recognition by Musashi-1 to design protein and RNA variants for in vitro and in vivo applications.

Nucleic acids research·2025

Related Experiment Video

Updated: Dec 18, 2025

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
07:24

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

2.1K

Paramagnetic NMR in drug discovery.

Charlotte A Softley1,2, Mark J Bostock1,2, Grzegorz M Popowicz1,2

  • 1Biomolecular NMR and Center for Integrated Protein Science Munich at Department Chemie, Technical University of Munich, Lichtenbergstraße 4, 85747, Garching, Germany.

Journal of Biomolecular NMR
|June 12, 2020
PubMed
Summary

Paramagnetic NMR uses unpaired electrons to generate structural restraints, aiding drug discovery. This technique enhances fragment screening and provides crucial structural data when crystallography is challenging.

Keywords:
Drug discoveryFragment screeningNuclear magnetic resonanceParamagnetic relaxation enhancementParamagnetismProtein–ligand structure determinationPseudo-contact shift

More Related Videos

High-Temperature and High-Pressure In situ Magic Angle Spinning Nuclear Magnetic Resonance Spectroscopy
08:55

High-Temperature and High-Pressure In situ Magic Angle Spinning Nuclear Magnetic Resonance Spectroscopy

Published on: October 9, 2020

5.9K
NMR-Based Fragment Screening in a Minimum Sample but Maximum Automation Mode
09:19

NMR-Based Fragment Screening in a Minimum Sample but Maximum Automation Mode

Published on: June 4, 2021

3.7K

Related Experiment Videos

Last Updated: Dec 18, 2025

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
07:24

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

2.1K
High-Temperature and High-Pressure In situ Magic Angle Spinning Nuclear Magnetic Resonance Spectroscopy
08:55

High-Temperature and High-Pressure In situ Magic Angle Spinning Nuclear Magnetic Resonance Spectroscopy

Published on: October 9, 2020

5.9K
NMR-Based Fragment Screening in a Minimum Sample but Maximum Automation Mode
09:19

NMR-Based Fragment Screening in a Minimum Sample but Maximum Automation Mode

Published on: June 4, 2021

3.7K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Medicinal Chemistry

Background:

  • Nuclear Magnetic Resonance (NMR) spectroscopy is vital in drug discovery for fragment screening and validating interactions.
  • Paramagnetic molecules possess unpaired electrons that influence NMR spectra, offering complementary structural information.
  • Standard structure calculation protocols can be enhanced with paramagnetic restraints.

Purpose of the Study:

  • To review strategies for incorporating paramagnetic centers into molecules for NMR studies.
  • To illustrate the utility of paramagnetic restraints in drug discovery through various examples.
  • To highlight the complementary nature of paramagnetic NMR to existing drug discovery techniques.

Main Methods:

  • Utilizing paramagnetic relaxation enhancements (PREs) for distance-dependent effects.
  • Employing pseudo-contact shift (PCS) restraints for both distance and angular information.
  • Introducing paramagnetic centers and analyzing their effects on NMR spectra.

Main Results:

  • Paramagnetic restraints enable more sensitive screening for weak-binding fragments.
  • This method provides essential structural insights for ligand poses when crystallography is difficult.
  • Paramagnetic NMR aids in filtering computational docking poses and generating interaction models.

Conclusions:

  • Paramagnetic NMR offers unique opportunities to overcome challenges in drug discovery, particularly for obtaining structural information.
  • Combining paramagnetic restraints with chemical shift perturbation and NOE data enhances structural determination.
  • Paramagnetic NMR is a valuable tool for complex drug discovery programs, especially when traditional methods fail.