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Related Concept Videos

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...
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...
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 Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

The spin state of an NMR-active nucleus can have a slight effect on its immediate electronic environment. This effect propagates through the intervening bonds and affects the electronic environments of NMR-active nuclei up to three bonds away; occasionally, even farther. This phenomenon is called spin–spin coupling or J-coupling. Coupling interactions are mutual and result in small changes in the absorption frequencies of both nuclei involved. While nuclei of the same element are involved in...
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...
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...

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Updated: May 24, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Cellular solid-state nuclear magnetic resonance spectroscopy.

Marie Renault1, Ria Tommassen-van Boxtel, Martine P Bos

  • 1Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands.

Proceedings of the National Academy of Sciences of the United States of America
|February 15, 2012
PubMed
Summary
This summary is machine-generated.

This study presents a novel solid-state Nuclear Magnetic Resonance (NMR) method. It reveals atomic-level details of molecular components within cells, advancing our understanding of cellular machinery.

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

Published on: October 9, 2020

Area of Science:

  • Structural Biology
  • Biophysics
  • Cellular Biology

Background:

  • Understanding cellular molecular machines is crucial for physiology.
  • Nuclear Magnetic Resonance (NMR) visualizes cellular entities at micrometer scale and provides 3D structures in vitro.
  • Existing methods have limitations in studying molecular components within their native cellular context at atomic resolution.

Purpose of the Study:

  • To introduce a solid-state NMR approach for atomic-level insights into cell-associated molecular components.
  • To enable simultaneous study of cellular compartments and associated proteins at atomic resolution.
  • To overcome limitations of current techniques for in-cell structural biology.

Main Methods:

  • Developed a solid-state NMR approach combining specialized protein production and labeling.
  • Utilized tailored solid-state NMR pulse sequences.
  • Applied the method to a recombinant integral membrane protein and endogenous bacterial components.

Main Results:

  • Achieved atomic-level structural insights into cell-associated molecular components.
  • Obtained structural information of a recombinant integral membrane protein within a bacterial environment.
  • Successfully analyzed major endogenous molecular components in bacteria.

Conclusions:

  • The novel solid-state NMR approach provides unprecedented atomic resolution for studying molecular components in their cellular context.
  • This method allows simultaneous investigation of entire cellular compartments and cell-associated proteins.
  • Opens new avenues for understanding fundamental physiological processes through in-cell structural biology.