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Related Experiment Video

Updated: May 21, 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

Solid-State NMR Approaches to Study Protein Structure and Protein-Lipid Interactions.

Christopher Aisenbrey¹, Evgeniy S Salnikov¹, Jesus Raya¹

¹Institut de Chimie, CNRS, Université de Strasbourg, UMR 7177, 4, Rue Blaise Pascal,, 67070, Strasbourg, France.

Methods in Molecular Biology (Clifton, N.J.)

|May 19, 2026

Summary

This summary is machine-generated.

Solid-state NMR spectroscopy provides high-resolution structural insights into membrane proteins within phospholipid bilayers. This technique, applicable to static samples, reveals the interdependence of lipids and proteins in the bilayer environment.

Keywords:

Bicelle Channel Cross polarization Detergent Helix topology Lee–Goldburg decoupling Membrane protein structure Membrane reconstitution Oriented bilayer PISEMA Protein insertion Separated local field spectroscopy Surface alignment Transmembrane orientation

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Last Updated: May 21, 2026

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

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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:

Biophysical Chemistry
Structural Biology
Membrane Protein Research

Background:

Solid-state NMR spectroscopy is crucial for studying membrane-associated polypeptides.
It offers high-resolution structural information in phospholipid bilayers, complementing solution-state NMR.
While traditionally used for peptides, the technique is advancing towards larger membrane proteins.

Purpose of the Study:

To present protocols for investigating membrane proteins using solid-state NMR.
To demonstrate the application of static, uniaxially oriented samples for structural analysis.
To explore the structure, dynamics, and topology of membrane polypeptides.

Main Methods:

Reconstitution of membrane proteins into oriented membranes.
Monitoring membrane alignment using 31P solid-state NMR spectroscopy.
1D and 2D 15N solid-state NMR for protein investigation and 2H solid-state NMR for lipid order parameters.

Main Results:

Detailed structural information of membrane proteins in oriented bilayers.
Insights into the dynamics and topology of membrane polypeptides.
Characterization of the interdependence between lipids and proteins within the bilayer.

Conclusions:

Solid-state NMR is a powerful technique for elucidating membrane protein structures.
The presented methods enable comprehensive analysis of protein-lipid interactions.
This approach enhances our understanding of the bilayer environment and its components.