Thermodynamic measurements of bilayer insertion of a single transmembrane helix chaperoned by fluorinated surfactants

Thermodynamic measurements of bilayer insertion of a single transmembrane helix chaperoned by fluorinated surfactants
Kyrychenko et al. 2012 (Alexey Ladokhin) - Journal of Molecular Biology

• Uses fluorinated surfactants to overcome peptide aggregation outside the membrane bilayer
• Study surfactant-chaperoned insertion into POPC vesicles with two WALP peptides: WALP23 and WALP27
• Meausres -9.0 + 0.1 and -10.0 + 0.1 kcal/mol for WALP23 and WALP27 respectively
• CD measurements confirm helicity
• Calculates 4-residue LALA segment in a helix costs ~1 kCal/mol to insert