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

4.4K
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.
4.4K
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

1.3K
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...
1.3K
¹H NMR of Labile Protons: Temporal Resolution01:10

¹H NMR of Labile Protons: Temporal Resolution

1.7K
Protons bonded to heteroatoms such as nitrogen and oxygen exhibit a range of chemical shift values. This is due to the varying degree of hydrogen bonding between the proton and the heteroatom in other molecules. The extent of hydrogen bonding affects the electron density around the proton, thereby giving different chemical shift values for the protons in the proton NMR spectrum.
The –OH proton in alcohols typically appears in the range of δ 2 to 5 ppm but can vary depending on the specific...
1.7K
Nuclear Magnetic Resonance (NMR): Overview01:07

Nuclear Magnetic Resonance (NMR): Overview

6.7K
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...
6.7K
Two-Dimensional (2D) NMR: Overview01:12

Two-Dimensional (2D) NMR: Overview

1.5K
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....
1.5K
Atomic Nuclei: Magnetic Resonance01:05

Atomic Nuclei: Magnetic Resonance

1.1K
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...
1.1K

You might also read

Related Articles

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

Sort by
Same author

Correction: Dynamic conformational equilibria in the active states of KRAS and NRAS.

RSC chemical biology·2026
Same author

A <sup>13</sup>C<sup>β</sup> CEST experiment with improved sensitivity for the characterization of protein excited states.

Journal of magnetic resonance (San Diego, Calif. : 1997)·2026
Same author

The dynamic and heterogeneous structure of the non-canonical inflammasome.

bioRxiv : the preprint server for biology·2026
Same author

Making invisible excited-state structures of pro-interleukin-18 visible by combining NMR and machine learning.

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

Structural heterogeneity and substrate engagement mechanism of the bacterial proteasome activator Bpa.

Nature communications·2026
Same author

Integration of computational and experimental techniques for the discovery of PL<sup>pro</sup> covalent inhibitors. When large virtual screening and rational design meet.

European journal of medicinal chemistry·2026
Same journal

Peptideins: Navigating the gray zone of the proteome.

Trends in biochemical sciences·2026
Same journal

A metabolon channels nicotine biosynthesis.

Trends in biochemical sciences·2026
Same journal

Better call chaperone.

Trends in biochemical sciences·2026
Same journal

Biochemistry at scale: Seeing both the forest and the trees.

Trends in biochemical sciences·2026
Same journal

Voices across Asia and Oceania: Biochemistry across borders.

Trends in biochemical sciences·2026
Same journal

Metabolic control of RNA splicing by polyamines.

Trends in biochemical sciences·2026
See all related articles

Related Experiment Video

Updated: Jan 18, 2026

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

2.7K

Observing biological dynamics at atomic resolution using NMR.

Anthony K Mittermaier1, Lewis E Kay

  • 1Department of Chemistry, McGill University, 801 Sherbrooke St. W., #322, Montreal, Quebec, Canada, H3A 2K6. anthony.mittermaier@mcgill.ca

Trends in Biochemical Sciences
|October 23, 2009
PubMed
Summary
This summary is machine-generated.

Biological macromolecules exhibit flexibility crucial for their function. New nuclear magnetic resonance (NMR) techniques reveal atomic-level insights into molecular motion, aiding the study of biological processes like binding and catalysis.

More Related Videos

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
08:03

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

2.5K
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

16.0K

Related Experiment Videos

Last Updated: Jan 18, 2026

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

2.7K
Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
08:03

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

2.5K
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

16.0K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Biological macromolecules display significant flexibility, undergoing conformational changes over various timescales.
  • Molecular dynamics are recognized as critical for macromolecular function.
  • The vast conformational space and infrequent, short-lived motions make studying the function-motion relationship challenging.

Purpose of the Study:

  • To explore the role of molecular dynamics in biological processes.
  • To investigate how recent advances in nuclear magnetic resonance (NMR) spectroscopy can elucidate these dynamics.
  • To gain atomic-level insights into fundamental biological mechanisms.

Main Methods:

  • Utilizing advanced solution nuclear magnetic resonance (NMR) spectroscopy.
  • Observing biomolecular dynamics with high resolution.
  • Applying NMR techniques to study processes like molecular binding and catalysis.

Main Results:

  • Demonstrated unprecedented detail in observing biomolecular dynamics.
  • Provided new insights into the relationship between molecular motion and function.
  • Enabled atomic-level understanding of biological processes.

Conclusions:

  • Advanced NMR spectroscopy is a powerful tool for dissecting molecular dynamics.
  • Understanding molecular motion is key to comprehending biological function at an atomic level.
  • These findings advance our knowledge of fundamental life processes.