Measurement of thermodynamic parameters for hydrophobic mismatch 2: intermembrane transfer of a transmembrane helix

Biochemistry
Yoshiaki YanoKatsumi Matsuzaki

Abstract

Hydrophobic matching between proteins and lipids is essential for the thermodynamic stability of integral membrane proteins. However, there is no direct thermodynamic information available about the intermembrane transfer of proteins between membranes with different hydrophobic thicknesses, which is crucial for understanding hydrophobic mismatch. This article reports the complete set of thermodynamic parameters (DeltaG, DeltaH, DeltaS, and DeltaC(p)) for the intermembrane transfer of the inert hydrophobic model transmembrane helix NBD-(AALALAA)(3)-NH(2) (NBD: 7-nitro-2-1,3-benzoxadiazol-4-yl), which is exchangeable between vesicles, from 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) to dimonounsaturated-phosphocholine lipid bilayers with different hydrophobic thicknesses (C14-C22) at 37-58 degrees C. The transfer free energies were calculated from equilibrium values of the extent of helix transfer from donor to acceptor lipid vesicles, as monitored by a decrease in fluorescence resonance energy transfer from the NBD group to a lipid-labeled Rhodamine in the donor upon transfer to the quencher-free acceptor. Under hydrophobic mismatch conditions up to approximately 7 A, the helix partitioning became unfavorable up to +...Continue Reading

References

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Citations

Feb 19, 2013·Chemistry and Physics of Lipids·Norberto CastilloD Peter Tieleman
Feb 1, 2008·Biophysical Journal·Derek Marsh
Apr 21, 2011·Biophysical Journal·Benjamin A HallMark S P Sansom
Aug 4, 2009·Biochimica Et Biophysica Acta·Yoshiaki Yano, Katsumi Matsuzaki
Feb 5, 2019·Yakugaku zasshi : Journal of the Pharmaceutical Society of Japan·Yoshiaki Yano, Katsumi Matsuzaki
Jan 21, 2010·The Journal of Physical Chemistry. B·Yoshiaki YanoKatsumi Matsuzaki

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