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Updated: Apr 3, 2026

Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases
Published on: November 21, 2010
Probing the gel to liquid-crystalline phase transition and relevant conformation changes in liposomes by (13)C
Rudra N Purusottam1, Lucile Sénicourt2, Jean-Jacques Lacapère2
1École Normale Supérieure, PSL Research University, Paris, France; Sorbonne Universités, UPMC University, Paris, France; CNRS, UMR 7203 LBM, Paris, France.
Abstract:
A straightforward way to visualize gel to liquid-crystalline phase transition in phospholipid membranes is presented by using ¹³C magic-angle spinning NMR. The changes in the 13C isotropic chemical shifts with increasing temperature are shown to be a sensitive probe of the main thermotropic phase transition related to lipid hydrocarbon chain dynamics and relevant conformational changes. The average value of the energy difference between trans and gauche states in the central C4–11 fragment of the DMPC acyl chain was estimated to be 4.02 ± 0.2 kJ mol⁻¹ in the liquid crystalline phase. The reported spectral features will be useful in 13C solid state NMR studies for direct monitoring of the effective lipid chain melting allowing rapid uniaxial rotation of membrane proteins in the biologically relevant liquid-crystalline phase.
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