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Article Dans Une Revue Biochimica et Biophysica Acta:Biomembranes Année : 2019

Minimal nanodisc without exogenous lipids for stabilizing membrane proteins in detergent-free buffer

Guy Schoehn

Résumé

Membrane protein stabilization after detergent solubilization presents drawbacks for structural and biophysical studies, in particular that of a reduced stability in detergent micelles. Therefore, alternative methods are required for efficient stabilization. Lipid nanodisc made with the membrane scaffold protein MSP is a valuable system but requires a fine optimization of the lipid to protein ratio. We present here the use of the scaffold protein MSP without added lipids as a minimal system to stabilize membrane proteins. We show that this method is applicable to α-helical and β-strands transmembrane proteins. This method allowed cryo-electron microscopy structural study of the bacterial transporter MexB. A protein quantification indicates that MexB is stabilized by two MSP proteins. This simplified and efficient method proposes a new advance in harnessing the MSP potential to stabilize membrane proteins.
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Dates et versions

hal-02070464 , version 1 (21-11-2020)

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Dimitri Salvador, Marie Glavier, Guy Schoehn, Gilles Phan, Jean-Christophe Taveau, et al.. Minimal nanodisc without exogenous lipids for stabilizing membrane proteins in detergent-free buffer. Biochimica et Biophysica Acta:Biomembranes, 2019, 1861 (4), pp.852-860. ⟨10.1016/j.bbamem.2019.01.013⟩. ⟨hal-02070464⟩
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