1. Inclusion of Lateral Pressure/Curvature Stress Effects in Implicit Membrane Models 
Huan Zhan, Themis Lazaridis 
Biophysical Journal 
Volume 104, Issue 3, Pages (February 2013)
DOI: /j.bpj
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2. Figure 1
The cross-sectional area of transmembrane and interfacial orientations of a (Gly)22 α-helix calculated as a sum of atomic contributions.
Biophysical Journal  , DOI: ( /j.bpj )
Copyright © 2013 Biophysical Society Terms and Conditions

3. Figure 2
The lateral pressure profile of a mixed DOPC/DOPE bilayer at different mole fractions of DOPE.
Biophysical Journal  , DOI: ( /j.bpj )
Copyright © 2013 Biophysical Society Terms and Conditions

4. Figure 3
The average configuration of (a) interfacial alamethicin, (b) transmembrane alamethicin, (c) melittin, (d) KB1, (e) 18A, (f) interfacial KKpL15, and (g) transmembrane KKpL15 at nP/nL = 0.01 and χ = 0. The average helix contents calculated based on the structures from our simulations are: 85% for alamethicin, 80% for melittin, 84% for 18A, and 75% for KKpL15, which are a little higher than the corresponding experimental values of 71–74% (84), 76% (84), 70–76% (76), and 65–75% (77). The structures do not change significantly with nP/nL or χ. The lines denote the hydrophobic boundary of the bilayers.
Biophysical Journal  , DOI: ( /j.bpj )
Copyright © 2013 Biophysical Society Terms and Conditions

5. Figure 4
(A) The relative binding energy of the peptides on mixed DOPC/DOPE bilayers at various mole fractions of DOPE. (B) The relative energy calculated with the average binding structures obtained at nP/nL = 0.01 and χ = 0.
Biophysical Journal  , DOI: ( /j.bpj )
Copyright © 2013 Biophysical Society Terms and Conditions