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Related Concept Videos

Applications Of NMR In Biology01:25

Applications Of NMR In Biology

4.0K
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.
4.0K
Nuclear Magnetic Resonance (NMR): Overview01:07

Nuclear Magnetic Resonance (NMR): Overview

3.9K
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...
3.9K
Atomic Nuclei: Magnetic Resonance01:05

Atomic Nuclei: Magnetic Resonance

766
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...
766
Double Resonance Techniques: Overview01:12

Double Resonance Techniques: Overview

310
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...
310
Two-Dimensional (2D) NMR: Overview01:12

Two-Dimensional (2D) NMR: Overview

901
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....
901
NMR Spectrometers: Resolution and Error Correction01:14

NMR Spectrometers: Resolution and Error Correction

784
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...
784

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Related Experiment Video

Updated: Sep 20, 2025

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

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Nanodiscs and solution nuclear magnetic resonance.

Olga Vinogradova1

  • 1University of Connecticut, School of Pharmacy, Department of Pharmaceutical Sciences, Storrs, CT 06269, USA.

Current Opinion in Structural Biology
|May 27, 2025
PubMed
Summary

Membrane protein structural studies are challenging. Solution nuclear magnetic resonance (NMR) in lipid nanodiscs offers recent advances for characterizing these vital proteins.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Membrane proteins are crucial genomic components and therapeutic targets.
  • High-resolution structural data for membrane proteins lag behind soluble proteins.
  • Studying membrane proteins in native-like environments remains difficult.

Purpose of the Study:

  • To review recent advancements in membrane protein characterization.
  • To highlight the application of solution nuclear magnetic resonance (NMR) methods.
  • To focus on the use of lipid nanodiscs for structural and dynamic studies.

Main Methods:

  • Solution nuclear magnetic resonance (NMR) spectroscopy.
  • Lipid nanodisc technology for membrane protein stabilization.
  • Structural and dynamic characterization techniques.

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Cryogenic Sample Loading into a Magic Angle Spinning Nuclear Magnetic Resonance Spectrometer that Preserves Cellular Viability
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Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
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Main Results:

  • Lipid nanodiscs provide native-like environments for membrane proteins.
  • Solution NMR enables high-resolution structural and dynamic insights.
  • Recent advances have improved the study of challenging membrane proteins.

Conclusions:

  • Lipid nanodiscs combined with solution NMR are powerful tools.
  • These methods advance the structural and dynamic understanding of membrane proteins.
  • This approach facilitates the study of key therapeutic targets.