Physics – Biological Physics
Scientific paper
2012-02-10
Physics
Biological Physics
Published in ACS Nano http://pubs.acs.org/doi/pdf/10.1021/nn204736b
Scientific paper
10.1021/nn204736b
Under dehydration conditions, amphipathic Late Embryogenesis Abundant (LEA) proteins fold spontaneously from a random conformation into alpha-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 alpha-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 (SCMF) theory show that the relative thickness of the stripes controls the free energy of interaction of the alpha-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.
Baulin Vladimir A.
Pogodin Sergey
Slater Nigel K. H.
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