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Related Concept Videos

Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
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.
Electron Microscope Tomography and Single-particle Reconstruction01:07

Electron Microscope Tomography and Single-particle Reconstruction

Transmission electron microscopy (TEM) can be used to determine the 3D structure of biological samples with the help of techniques such as electron microscope tomography and single-particle reconstruction. While single-particle reconstruction can examine macromolecules and macromolecular complexes in vitro conditions only, tomography permits the study of cell components or small cells in vivo.
Electron Tomography
Electron tomography can be performed either in TEM or STEM (scanning transmission...

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Related Experiment Video

Updated: Jun 11, 2026

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the &#181;s-ms Timescale
08:09

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale

Published on: April 19, 2021

Combining methods for speeding up multi-dimensional acquisition. Sparse sampling and fast pulsing methods for

Dominique Marion1

  • 1Laboratoire de RMN, Institut de Biologie Structurale Jean-Pierre Ebel, UMR5075 CNRS-CEA-UJF, 41, Rue Jules Horowitz, 38027 Grenoble Cedex, France. Dominique.Marion@ibs.fr

Journal of Magnetic Resonance (San Diego, Calif. : 1997)
|July 3, 2010
PubMed
Summary

High-resolution 4D NMR spectra aid intrinsically disordered protein resonance assignment. Adapted BEST-experiments with sparse sampling and maximum entropy reconstruction enable faster, detailed analysis of these challenging protein structures.

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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

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Last Updated: Jun 11, 2026

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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

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

Published on: September 17, 2017

Area of Science:

  • Structural Biology
  • Nuclear Magnetic Resonance (NMR) Spectroscopy

Background:

  • Intrinsically disordered proteins (IDPs) present significant challenges for resonance assignment due to extensive spectral overlaps.
  • High-resolution multidimensional NMR spectra are crucial for characterizing IDPs.

Purpose of the Study:

  • To adapt existing 3D BEST-experiments for improved resonance assignment in unfolded proteins.
  • To enhance spectral resolution and data acquisition efficiency for IDPs.

Main Methods:

  • Implementation of semi-constant time evolution and sparse sampling in 3D BEST-experiments.
  • Application of maximum entropy reconstruction to mitigate artifacts from sparse sampling.
  • Development of a 4D NMR experiment for IDP analysis.

Main Results:

  • Reduced artifact intensity in spectra, comparable to other noise sources.
  • Achieved reasonable spectral resolution in a 4D experiment.
  • Acquisition time for the 4D experiment was reduced to under 60 hours.

Conclusions:

  • Adapted BEST-experiments provide a viable method for high-resolution NMR analysis of IDPs.
  • The developed methodology significantly improves the efficiency and resolution of resonance assignment for unfolded proteins.
  • This approach facilitates detailed structural insights into IDPs.