[button href="http://pubs.acs.org/doi/pdf/10.1021/nn204736b" color="lime_green" target="_blank" id=""]PDF[/button]
[button href="http://arxiv.org/pdf/1202.2310v1" color="sea_foam" target="_blank" id=""]arXiv[/button]
S. Pogodin, N. K. H. Slater and V. A. Baulin
ACS Nano, 6(2), 1308-1313 (2012)
Under dehydration conditions, amphipathic late embryogenesis abundant proteins fold spontaneously from a random conformation into α-helical structures, and this transition is promoted by the presence of membranes. To gain insight into the thermodynamics of membrane association, we model the resulting α-helical structures as infinite rigid cylinders patterned with hydrophobic and hydrophilic stripes oriented parallel to their axis. Statistical thermodynamic calculations using single chain mean field theory show that the relative thickness of the stripes controls the free energy of interaction of the α-helices with a phospholipid bilayer, as does the bilayer structure and the depth of the equilibrium penetration of the cylinders into the bilayer. The results may suggest the optimal thickness of the stripes to mimic the association of such protein with membranes.