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Related Concept Videos

NMR Spectrometers: Overview01:20

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

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.
¹H NMR Signal Multiplicity: Splitting Patterns01:13

¹H NMR Signal Multiplicity: Splitting Patterns

When protons A and X are coupled, their nuclear spin energy levels are slightly modified. This is because the energy required to excite proton A to a spin state parallel to proton X is slightly different from the energy required for it to become anti-parallel to spin X. Consequently, there are two possible excitation frequencies for A (A1 and A2), depending on the spin state of X, and vice versa. The mutual nature of coupling implies that the difference between frequencies A1 and A2, indicated...
NMR Spectrometers: Radiofrequency Pulses and Pulse Sequences01:17

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.
Applications Of NMR In Biology01:25

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 Heteronuclear Correlation Techniques01:18

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.

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Related Experiment Video

Updated: Jul 12, 2026

Metabolomic Analysis of Rat Brain by High Resolution Nuclear Magnetic Resonance Spectroscopy of Tissue Extracts
09:01

Metabolomic Analysis of Rat Brain by High Resolution Nuclear Magnetic Resonance Spectroscopy of Tissue Extracts

Published on: September 21, 2014

High-resolution iterative frequency identification for NMR as a general strategy for multidimensional data

Hamid R Eghbalnia1, Arash Bahrami, Marco Tonelli

  • 1National Magnetic Resonance Facility at Madison, Center for Eukaryotic Structural Genomics, Graduate Program in Biophysics, Biochemistry Department, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA. eghbalni@nmrfam.wisc.edu

Journal of the American Chemical Society
|September 8, 2005
PubMed
Summary

High-resolution iterative frequency identification for NMR (HIFI-NMR) rapidly collects and processes multidimensional NMR data. This novel approach significantly reduces data collection time and processing, achieving high accuracy for protein resonance assignment.

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Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)
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Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)

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

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Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)
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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

Area of Science:

  • Nuclear Magnetic Resonance (NMR) Spectroscopy
  • Structural Biology
  • Computational Chemistry

Background:

  • Multidimensional NMR is crucial for determining protein structure and dynamics.
  • Current methods for data collection and processing can be time-consuming and computationally intensive.
  • Reduced dimensionality approaches offer faster data acquisition but require efficient processing algorithms.

Purpose of the Study:

  • To introduce a novel, rapid approach for multidimensional NMR data collection and processing called HIFI-NMR.
  • To develop an algorithm that adaptively selects data collection planes and statistically models spectral space.
  • To enable direct generation of probabilistic peak lists for efficient protein resonance assignment.

Main Methods:

  • HIFI-NMR collects n-dimensional data as a series of 2D planes, adaptively selecting tilted planes based on statistical analysis.
  • An online algorithm models 3D peak positions probabilistically, optimizing the next plane selection and determining data collection termination.
  • Robust statistical algorithms process plane projections to drive data collection and directly generate peak lists with associated probabilities.

Main Results:

  • HIFI-NMR successfully identified approximately 98% of real peaks in 3D triple-resonance experiments for both small and large proteins.
  • Data collection time was reduced by approximately tenfold compared to conventional 3D NMR methods.
  • The method directly generated peak lists with probabilities, bypassing extensive post-acquisition processing and peak-picking.

Conclusions:

  • HIFI-NMR offers a significant advancement in the speed and efficiency of multidimensional NMR data acquisition and processing.
  • The approach is highly accurate, comparable to conventional methods, while drastically reducing experimental time.
  • HIFI-NMR is implementable on commercial spectrometers and extensible to higher-dimensional NMR studies, facilitating faster protein structure determination.