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Related Concept Videos

Nuclear Magnetic Resonance (NMR): Overview01:07

Nuclear Magnetic Resonance (NMR): Overview

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...
Atomic Nuclei: Magnetic Resonance01:05

Atomic Nuclei: Magnetic Resonance

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...
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...
NMR Spectrometers: Resolution and Error Correction01:14

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...
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...
Double Resonance Techniques: Overview01:12

Double Resonance Techniques: Overview

Double resonance techniques in Nuclear Magnetic Resonance (NMR) spectroscopy involve the simultaneous application of two different frequencies or radiofrequency pulses to manipulate and observe two distinct nuclear spins. One important application of double resonance is spin decoupling, which selectively suppresses coupling with one type of nucleus while observing the NMR signal from another nucleus, simplifying the spectrum and enhancing resolution.
Spin decoupling is usually achieved by...

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Updated: May 17, 2026

High-Temperature and High-Pressure In situ Magic Angle Spinning Nuclear Magnetic Resonance Spectroscopy
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High-Temperature and High-Pressure In situ Magic Angle Spinning Nuclear Magnetic Resonance Spectroscopy

Published on: October 9, 2020

Solution nuclear magnetic resonance spectroscopy.

James J Chou1, Remy Sounier

  • 1Jack and Eileen Connors Structural Biology Laboratory, Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, USA.

Methods in Molecular Biology (Clifton, N.J.)
|November 8, 2012
PubMed
Summary
This summary is machine-generated.

Solution nuclear magnetic resonance (NMR) spectroscopy advances protein structure determination, offering insights into dynamics and interactions. This versatile technique complements X-ray and electron microscopy for biological structure and function studies.

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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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Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)
10:28

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

Published on: November 2, 2018

Area of Science:

  • Biochemistry and structural biology
  • Biophysical techniques
  • Molecular dynamics

Background:

  • Solution nuclear magnetic resonance (NMR) spectroscopy has significantly evolved over 30 years for biological molecule characterization.
  • NMR structures in the Protein Data Bank (9,521 as of Sep 1, 2012) are growing, though fewer than crystallographic methods (74,009).
  • NMR structure determination relies on measuring restraints and finding solutions, differing from Fourier optics-based X-ray and electron microscopy methods.

Purpose of the Study:

  • To highlight the advancements and versatility of solution NMR spectroscopy in structural biology.
  • To discuss the application of NMR in studying protein dynamics, interactions, folding, and conformational changes.
  • To emphasize the growing role of NMR in membrane protein structural studies and its future potential.

Main Methods:

  • Utilizes nuclear magnetic resonance (NMR) principles to measure structural restraints.
  • Employs advanced spectrometer technology, pulse experiments, and isotope labeling schemes.
  • Leverages specialized software for structure determination from NMR data.

Main Results:

  • NMR is capable of high-precision de novo structure determination.
  • NMR measurements under physiological conditions provide direct functional insights.
  • NMR is increasingly effective for membrane proteins, including ion channels and receptors.
  • Hardware advancements, like cryogenic probes, reduce required sample concentrations.

Conclusions:

  • Solution NMR is a versatile tool for mechanistic and structural biology questions.
  • The method is crucial for studying protein dynamics, interactions, and intrinsically unfolded proteins.
  • Solution NMR is poised for significant growth, complementing X-ray and EM in protein structure and function research.