Sergey Pogodin, Nigel K. H. Slater, Vladimir A. Baulin
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.
View original:
http://arxiv.org/abs/1202.2310
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