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

Applications Of NMR In Biology

Applications Of NMR In Biology

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.
The...

2D NMR: Overview of Homonuclear Correlation Techniques

2D NMR: Overview of Homonuclear Correlation Techniques

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...

2D NMR: Overview of Heteronuclear Correlation Techniques

2D NMR: Overview of Heteronuclear Correlation Techniques

Heteronuclear correlation spectroscopy is an analytical technique that investigates the coupling between different types of nuclei, often a proton and an X-nucleus, such as carbon-13 or nitrogen-15. This method is commonly used in nuclear magnetic resonance (NMR) spectroscopy to gain insights into complex chemical compounds' structural and compositional aspects. A typical heteronuclear correlation spectrum displays X-nucleus chemical shifts on one axis and a proton spectrum on the other axis.

NMR Spectrometers: Overview

NMR Spectrometers: Overview

NMR spectrometers consist of a strong magnet, a radiofrequency transmitter, and a detector attached to a computer console for recording spectra of samples containing NMR-active nuclei. In first-generation NMR instruments called continuous-wave spectrometers, the resonance frequencies of the nuclei are determined by frequency-sweep or field-sweep methods. The magnetic field strength is fixed and the rf signal is swept in the former, while the radiofrequency signal is fixed and the magnetic field...

¹H NMR: Interpreting Distorted and Overlapping Signals

¹H NMR: Interpreting Distorted and Overlapping Signals

Spin systems where the difference in chemical shifts of the coupled nuclei is greater than ten times J are called first-order spin systems. These nuclei are weakly coupled, and their chemical shifts and coupling constant can generally be estimated from the well-separated signals in the spectrum.
As Δν decreases and the signals move closer, the doublets appear increasingly distorted. The intensities of the inner lines increase at the cost of those of the outer lines as the signals are slanted or...

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

Other Nuclides: ³¹P, ¹⁹F, ¹⁵N NMR

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 high...

You might also read

Related Articles

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

Sort by

Same author

Site-Specific Hydrogen-Deuterium Exchange Mass Spectrometry for Deep Explorations of Dynamic Shifts in Protein-Drug Interactions.

Journal of the American Chemical Society·2026

Same author

Decoding Enzyme-Inhibitor Kinetic Mechanisms by Isothermal Titration Calorimetry: The Case of SARS-CoV-2 3CL<sup>pro</sup>.

Analytical chemistry·2026

Same author

Assessing Metal Ion Assignment Accuracy in Protein Data Bank Models via Elemental Spectroscopy.

Journal of chemical information and modeling·2026

Same author

Allosteric Protein Chemical Shift Perturbations are Ubiquitous.

bioRxiv : the preprint server for biology·2026

Same author

The NMR Exchange Format (NEF): Specification and Applications.

bioRxiv : the preprint server for biology·2026

Same author

Hidden structural states of proteins revealed by conformer selection.

Nature communications·2026

Search research articles

Related Experiment Video

Updated: Jun 24, 2026

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

Unique opportunities for NMR methods in structural genomics.

Gaetano T Montelione¹, Cheryl Arrowsmith, Mark E Girvin

¹Center for Advanced Biotechnology and Medicine, Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, NJ 08854, USA. guy@cabm.rutgers.edu

Journal of Structural and Functional Genomics

|March 17, 2009

Summary

This summary is machine-generated.

Nuclear Magnetic Resonance (NMR) spectroscopy has been crucial for the United States Protein Structure Initiative (PSI). New NMR methods are advancing protein structure determination and impacting the wider scientific community.

More Related Videos

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance

Published on: August 26, 2025

Mass Spectrometry-Guided Genome Mining as a Tool to Uncover Novel Natural Products

Mass Spectrometry-Guided Genome Mining as a Tool to Uncover Novel Natural Products

Published on: March 12, 2020

Related Experiment Videos

Last Updated: Jun 24, 2026

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

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance

Published on: August 26, 2025

Mass Spectrometry-Guided Genome Mining as a Tool to Uncover Novel Natural Products

Mass Spectrometry-Guided Genome Mining as a Tool to Uncover Novel Natural Products

Published on: March 12, 2020

Area of Science:

Biochemistry
Structural Biology
Biophysics

Background:

The United States Protein Structure Initiative (PSI) aimed to determine the three-dimensional structures of proteins.
Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful technique for studying protein structure and dynamics.

Purpose of the Study:

To provide an overview of NMR's role in the PSI.
To outline the future contributions of NMR to the PSI-Biology program.

Main Methods:

Perspective based on a workshop held in July 2008.
Review of NMR's contributions to protein structure production within the PSI.

Main Results:

NMR has played a significant role in the PSI's structure production efforts.
Development of novel NMR methods has advanced the field of protein NMR.

Conclusions:

NMR spectroscopy has been integral to the success of the PSI.
Emerging NMR techniques will be vital for the upcoming PSI-Biology program and the broader protein NMR community.