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

Two-Dimensional (2D) NMR: Overview

Two-Dimensional (2D) NMR: Overview

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.

2D NMR: Homonuclear Correlation Spectroscopy (COSY)

2D NMR: Homonuclear Correlation Spectroscopy (COSY)

Homonuclear correlation spectroscopy, or COSY, is a 2-dimensional NMR technique that provides information about coupled protons. Typically, the geminal and vicinal coupling are observed. For example, consider the COSY spectrum of ethyl acetate, where its 1D proton NMR spectrum is plotted along the vertical and horizontal axes with their corresponding chemical shift scale. Three spots on the diagonal corresponding to the three peaks in the 1D proton spectrum are called diagonal peaks. The COSY...

2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)

2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)

Heteronuclear single-quantum correlation spectroscopy (HSQC) is a 2D NMR technique that reveals one-bond correlations between hydrogen and a heteronucleus. The HSQC experiment is similar to the heteronuclear correlation experiment (HETCOR) but is more sensitive. In the HSQC spectrum, the proton chemical shift is plotted on the horizontal F2 axis, while the 13C chemical shift is plotted on the vertical F1 axis. The corresponding proton and 13C spectra are also shown. The HSQC contour plot does...

NMR Spectroscopy Of Amines

NMR Spectroscopy Of Amines

In proton NMR spectroscopy, primary amines and secondary amines showcase their N–H protons as a broad signal in the chemical shift range between δ 0.5 and 5 ppm. The exact position in this range depends on several factors, including sample concentration, hydrogen bonding, and the type of solvent used. Since amine protons undergo fast proton exchange in solution, the protons are labile and therefore do not participate in any splitting with adjacent protons. Thus, the observed peak is broad and...

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.

You might also read

Related Articles

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

Sort by

Same author

Autoimmune Hemolytic Anemia Following Intravenous Immunoglobulin in Kawasaki Disease.

Cureus·2026

Same author

Moving NMR infrastructures to remote access capabilities.

Progress in nuclear magnetic resonance spectroscopy·2026

Same author

Unmet HIV and STI Prevention Needs and Limited Linkage to Care Among Gay, Bisexual, and Other Men Who Have Sex with Men in Southern Spain: A Community-Based Intervention Study.

AIDS patient care and STDs·2026

Same author

Oligomerization enables the selective targeting of an intrinsically disordered region by a small molecule.

Science advances·2026

Same author

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

Solid state nuclear magnetic resonance·2025

Same author

Equine Infectious Anemia Virus in Equids: A Large-Scale Serosurvey in Western Europe.

Animals : an open access journal from MDPI·2025

Search research articles

Related Experiment Video

Updated: Jul 25, 2026

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

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

Published on: June 4, 2021

Fast 2D NMR ligand screening using Hadamard spectroscopy.

Miguel Feliz¹, Jesús García, Eric Aragón

¹Laboratory of Biomolecular NMR, Institute of Research in Biomedicine, Science Research Park, Josep Samitier 1-5, 08028 Barcelona, Spain.

Journal of the American Chemical Society

|June 1, 2006

Summary

Hadamard encoded spectroscopy enables rapid 2D NMR screening by focusing on specific signals. This method quantifies ligand-induced shifts using peak intensities from a Hadamard constellation, accelerating drug discovery.

More Related Videos

Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue

Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue

Published on: May 17, 2024

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance

Published on: August 26, 2025

Related Experiment Videos

Last Updated: Jul 25, 2026

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

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

Published on: June 4, 2021

Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue

Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue

Published on: May 17, 2024

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance

Published on: August 26, 2025

Area of Science:

Biophysical Chemistry
Structural Biology
Chemical Biology

Background:

Nuclear Magnetic Resonance (NMR) spectroscopy is crucial for molecular characterization.
Efficient screening methods are needed to identify molecular interactions, particularly in drug discovery.
Targeting specific sites like enzyme active or ligand recognition sites enhances screening specificity.

Purpose of the Study:

To develop a fast 2D NMR-based screening method.
To enable focused analysis of specific molecular signals.
To quantify ligand-induced chemical shifts accurately.

Main Methods:

Utilized Hadamard encoded spectroscopy for 2D NMR.
Acquired a set of Hadamard spectra (Hadamard constellation) with specific offsets.
Analyzed peak intensities to determine quantitative ligand-induced shifts.

Main Results:

Achieved fast 2D NMR-based screening.
Successfully focused on signals from enzyme active or ligand recognition sites.
Quantified ligand-induced shifts accurately from peak intensities.

Conclusions:

Hadamard encoded spectroscopy provides an efficient approach for 2D NMR screening.
The method allows for precise quantification of ligand-induced shifts.
This technique can accelerate the identification of molecular interactions and potential drug candidates.