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Updated: Feb 25, 2026
Neutron Spin Echo Spectroscopy as a Unique Probe for Lipid Membrane Dynamics and Membrane-Protein Interactions
Published on: May 27, 2021
Solid-State NMR of Membrane Protein Reconstituted in Proteoliposomes, the Case of TSPO
Lucile Senicourt1, Luminita Duma2, Vassilios Papadopoulos3,4
1Sorbonne Universités-UPMC University of Paris 06, Département de Chimie, École Normale Supérieure-PSL Research University, CNRS UMR 7203 LBM, 4 Place Jussieu, 75005, Paris Cedex 05, France.
Abstract:
Structural studies of membrane proteins (MP) in a native or native-like environment remain a challenge. X-ray crystallography of three-dimensional crystals of MP in lipids and cryo-electron microscopy of two-dimensional crystals also in lipids have given atomic structures of several MP. Recent developments of solid-state NMR (ssNMR) provided structural data of MP in lipids and should give access to the dynamic behavior of MP's in a native-like environment. Preparation of samples for ssNMR is not trivial with overexpressed proteins since purified recombinant MP have to be reincorporated in proteoliposomes and concentrated in the small volume of the rotor used for ssNMR studies. We present here the protocol that we have used to study the recombinant mouse TSPO1, an integral membrane protein of 20 kDa mostly found in the outer membrane of mitochondria and overexpressed in E. coli bacteria.
