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¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

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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...

Atomic Nuclei: Nuclear Spin State Overview

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NMR-active nuclei have energy levels called 'spin states' that are associated with the orientations of their nuclear magnetic moments. In the absence of a magnetic field, the nuclear magnetic moments are randomly oriented, and the spin states are degenerate. When an external magnetic field is applied, the spin states have only 2 + 1 orientations available to them. A proton with = ½ has two available orientations. Similarly, for a quadrupolar nucleus with a nuclear spin value of one, the...

Atomic Nuclei: Magnetic Resonance

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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...

¹H NMR: Interpreting Distorted and Overlapping Signals

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Spin systems where the difference in chemical shifts of the coupled nuclei is greater than ten times J are called first-order spin systems. These nuclei are weakly coupled, and their chemical shifts and coupling constant can generally be estimated from the well-separated signals in the spectrum.
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Related Experiment Video

Updated: Apr 12, 2026

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

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

Published on: September 17, 2017

Magic-angle-spinning solid-state NMR of membrane proteins.

Lindsay A Baker¹, Gert E Folkers¹, Tessa Sinnige¹

¹NMR Spectroscopy, Bijvoet Center for Biomolecular Research, Department of Chemistry, Faculty of Science, Utrecht University, Utrecht, The Netherlands.

Methods in Enzymology

|May 8, 2015

Summary

Solid-state NMR spectroscopy (ssNMR) enables detailed studies of membrane proteins in various environments. Optimized ssNMR methods reveal membrane protein structure and function, advancing research in cellular systems.

Keywords:

Cellular envelope Dynamic nuclear polarization Ion channel Membrane proteins Proteoliposome Solid-state NMR β-Barrel protein

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Neutron Spin Echo Spectroscopy as a Unique Probe for Lipid Membrane Dynamics and Membrane-Protein Interactions

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Last Updated: Apr 12, 2026

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

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Published on: September 17, 2017

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

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Published on: October 9, 2020

Neutron Spin Echo Spectroscopy as a Unique Probe for Lipid Membrane Dynamics and Membrane-Protein Interactions

Neutron Spin Echo Spectroscopy as a Unique Probe for Lipid Membrane Dynamics and Membrane-Protein Interactions

Published on: May 27, 2021

Area of Science:

Biophysics
Structural Biology
Spectroscopy

Background:

Membrane proteins are crucial for cellular functions but challenging to study.
Solid-state NMR spectroscopy (ssNMR) offers unique capabilities for investigating membrane proteins in diverse settings.

Purpose of the Study:

To discuss experimental aspects and methodologies for ssNMR studies of membrane proteins.
To highlight how ssNMR can correlate protein structure with function in various molecular environments.

Main Methods:

Protein expression, labeling, and isolation strategies.
ssNMR experiments utilizing magic-angle-spinning, filtering, and correlation techniques.
Consideration of sample preparation, sensitivity, and spectral resolution.

Main Results:

Optimized procedures for protein expression, purification, and refolding are essential.
Native membrane samples can simplify biochemical challenges.
ssNMR approaches provide structural insights and functional information for membrane proteins in lipid bilayers.

Conclusions:

ssNMR is a powerful technique for studying membrane protein structure and function.
Advancements in sample preparation and NMR methodology will further enhance ssNMR's potential for cellular membrane protein systems.