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Updated: May 27, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
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NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

Membrane protein structure and dynamics from NMR spectroscopy.

Mei Hong1, Yuan Zhang, Fanghao Hu

  • 1Department of Chemistry, Iowa State University, Ames, 50011, USA. mhong@iastate.edu

Annual Review of Physical Chemistry
|December 6, 2011
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Summary

Solid-state NMR determines membrane protein structures in lipid bilayers, revealing dynamics and interactions. Comparing these with solution NMR structures highlights environmental effects on protein conformation.

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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Published on: September 17, 2017

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Last Updated: May 27, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
09:25

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

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:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Membrane proteins are crucial biological components with complex structures.
  • Determining membrane protein structures is challenging due to their hydrophobic nature and native environment.
  • Solid-state NMR spectroscopy offers a powerful tool for structural analysis within lipid bilayers.

Purpose of the Study:

  • To review the capabilities of solid-state NMR for membrane protein structure determination.
  • To highlight the types of structural constraints measurable by solid-state NMR.
  • To discuss the insights gained from comparing solid-state NMR structures with solution NMR structures.

Main Methods:

  • Multidimensional magic-angle-spinning correlation NMR spectroscopy.
  • Oriented-sample experiments in lipid bilayers.
  • Application to various membrane protein classes including channels, pumps, and receptors.

Main Results:

  • Solid-state NMR enables measurement of torsion angles, interatomic distances, and oligomeric states.
  • Protein dynamics, ligand interactions, and membrane insertion depth can be elucidated.
  • Structures of diverse membrane proteins like potassium channels and GPCRs have been determined.

Conclusions:

  • Solid-state NMR is a key technique for high-resolution membrane protein structure determination in native-like environments.
  • Structural data from solid-state NMR provide insights into protein function and mechanism.
  • Comparison with solution NMR structures reveals the influence of detergent environments on membrane protein conformation.