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.

NMR Spectrometers: Resolution and Error Correction

NMR Spectrometers: Resolution and Error Correction

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...

NMR Spectrometers: Radiofrequency Pulses and Pulse Sequences

NMR Spectrometers: Radiofrequency Pulses and Pulse Sequences

A pulse is a short burst of radio waves distributed over a range of frequencies that simultaneously excites all the nuclei in the sample. Upon passing a radio frequency pulse along the x-axis, the nuclei absorb energy corresponding to their Larmor frequencies and achieve resonance. This shifts the net magnetization vector from the z-axis toward the transverse plane. This angle of rotation of the magnetization vector, or the flip angle, is proportional to the duration and intensity of the pulse.

Sampling Theorem

Sampling Theorem

In signal processing, the analysis of continuous-time signals, denoted as x(t), often involves sampling techniques to convert these signals into discrete-time signals. This process is essential for digital representation and manipulation. A critical component in sampling is the train of impulses, characterized by the sampling interval and the sampling frequency. The relationship between these parameters and the original signal's properties dictates the success of the sampling process.

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...

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

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...

You might also read

Related Articles

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

Sort by

Same author

A Lipid-Conjugation Strategy for Intracellular Reactive Oxygen Species Control in Hepatic Cells.

Angewandte Chemie (International ed. in English)·2026

Same author

Moving NMR infrastructures to remote access capabilities.

Progress in nuclear magnetic resonance spectroscopy·2026

Same author

Accordion-like tuning of composite pulse dipolar recoupling in solid-state NMR.

The Journal of chemical physics·2026

Same author

Mobility of lactose in Milk powders.

Food research international (Ottawa, Ont.)·2026

Same author

Longitudinal Pulsed Dynamic Nuclear Polarization Transfer via Periodic Optimal Control.

The journal of physical chemistry letters·2026

Same author

Selective Mineral Recovery from Seawater by Ion-Exchangeable Metal-Organic Framework Glasses.

Journal of the American Chemical Society·2026

Search research articles

Related Experiment Video

Updated: Jun 23, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

NMR ¹⁵N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

Defining the sampling space in multidimensional NMR experiments: what should the maximum sampling time be?

Thomas Vosegaard¹, Niels Chr Nielsen

¹Center for Insoluble Protein Structures (inSPIN), Interdisciplinary Nanoscience Center (iNANO) and Department of Chemistry, University of Aarhus, Aarhus C, Denmark. tv@chem.au.dk

Journal of Magnetic Resonance (San Diego, Calif. : 1997)

|May 12, 2009

Summary

Optimizing sampling times in multidimensional NMR experiments balances spectral quality and experiment duration. This study analyzes sampling strategies to improve efficiency in nuclear magnetic resonance spectroscopy.

More Related Videos

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

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

Published on: September 23, 2021

Related Experiment Videos

Last Updated: Jun 23, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

NMR ¹⁵N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

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

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

Published on: September 23, 2021

Area of Science:

Nuclear Magnetic Resonance (NMR) Spectroscopy
Signal Processing
Physical Chemistry

Background:

Efficient signal sampling is crucial for optimizing multidimensional NMR experiments.
Balancing experiment time and spectral quality is a key challenge.
Standard rectangular sampling and Fourier transformation are widely used.

Purpose of the Study:

To determine the optimal maximum sampling time in individual dimensions for multidimensional NMR.
To analyze the impact of sampling time on spectral resolution and experiment duration.
To propose efficient sampling strategies for typical NMR scenarios.

Main Methods:

Theoretical analysis of the sampling space problem.
Numerical simulations of sampling strategies.
Experimental validation of proposed approaches.

Main Results:

Identification of optimal sampling times for improved spectral resolution.
Demonstration of reduced experiment times through efficient sampling.
Validation of theoretical models with numerical and experimental data.

Conclusions:

Efficient sampling strategies can significantly enhance multidimensional NMR experiments.
The proposed methods offer a practical approach to optimizing sampling in NMR.
This work contributes to improving the efficiency and quality of NMR data acquisition.