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Related Concept Videos

¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR

The axial and equatorial protons in cyclohexane can be distinguished by performing a variable-temperature NMR experiment. In this process, except for one proton, the remaining eleven protons are replaced by deuterium. The deuterium substitution avoids the possible peak splitting caused by the spin-spin coupling between the adjacent protons. The remaining proton flips between the axial and equatorial positions.
Two-Dimensional (2D) NMR: Overview01:12

Two-Dimensional (2D) NMR: Overview

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.
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...

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Related Experiment Video

Updated: Jun 10, 2026

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

Determination of membrane protein structures using solution and solid-state NMR.

Pierre Montaville1, Nadège Jamin

  • 1CEA, iBiTecs, URA 2096, SB2SM, Gif-sur-Yvette, France.

Methods in Molecular Biology (Clifton, N.J.)
|July 29, 2010
PubMed
Summary

Nuclear Magnetic Resonance (NMR) is crucial for biomolecule characterization. Recent advances enhance membrane protein (MP) structure determination using solution and solid-state NMR, overcoming previous challenges.

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Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
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Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

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Last Updated: Jun 10, 2026

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

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

Area of Science:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • Nuclear Magnetic Resonance (NMR) is vital for atomic-level biomolecular structure, dynamics, and interaction studies.
  • Applying NMR to membrane proteins (MPs) presents significant challenges, including low sensitivity, size limitations, and intrinsic motion.

Purpose of the Study:

  • To review recent advancements in NMR techniques for membrane protein (MP) structure determination.
  • To highlight the challenges and specific requirements of solution and solid-state NMR (ssNMR) for MPs.
  • To emphasize the potential of NMR in providing atomic-level insights into MP structure and function.

Main Methods:

  • Utilizing solution NMR with specific detergent selection and stable isotope labeling for distance restraints.
  • Employing solid-state NMR (ssNMR) for atomic-level information, including membrane protein orientation.
  • Developing advanced sample preparation and labeling strategies for ssNMR spectra assignment and distance measurements.

Main Results:

  • Recent progress has accelerated the release of high-resolution MP structures.
  • NMR now provides unprecedented structural and dynamics information for MPs.
  • ssNMR offers unique insights into MP orientation within phospholipid bilayers.

Conclusions:

  • NMR, particularly with recent advances, is a powerful and increasingly accessible tool for studying membrane protein structure and dynamics.
  • Overcoming challenges in sensitivity, size, and motion has significantly improved MP structure determination.
  • The integration of solution and ssNMR methodologies provides comprehensive insights into membrane protein function.