Dependence of lipid membrane phase transition temperature on the mismatch of protein and lipid hydrophobic thickness
Research output: Contribution to journal › Journal article › peer-review
A two-component solution theory is studied which incorporates hydrophobic matching as a major contribution to the lipid-protein interactions in biological membranes. A special geometrical constraint has been discovered which has important implications for the quantitative interpretation of physical effects to lipid-protein interactions. The theory has an advantage over conventional Landau-type phenomenological descriptions in that it accounts for phase separation. A certain class of experimental systems, photosynthetic reaction centre and antenna proteins reconstituted into synthetic lipid membranes of different hydrophobic thicknesses, are considered with a view to determining the parameters of the theory. The theoretical predictions are found to be in good agreement with experimental measurements of shifts in the phase transition temperature.
Original language | English |
---|---|
Journal | European Biophysics Journal |
Volume | 16 |
Issue number | 1 |
Pages (from-to) | 1-10 |
Number of pages | 10 |
ISSN | 0175-7571 |
DOIs | |
Publication status | Published - 1988 |
Externally published | Yes |
- hydrophobic thickness, lipid membrane, lipid-protein interactions, membrane elasticity, phase diagram, solution theory
Research areas
ID: 238390765