Figure 6. Dimerization of two peripheral membrane proteins in opposing leaflets.
(a) Representative potentials of mean force, 
, of two PMPs (
) residing in opposing leaflets. For combinations of sufficiently short proteins (
, black curve; 
, red curve) the minimum of 
emerges at vanishing distances. For 
a slight increase of 
is observed as a result of the PMPs' construction via finite beads, i.e. configuration (i) is energetically less favorable than arrangement (ii). For longer proteins (
, green curve), a side-by-side arrangement of PMPs is observed, and the minimum of 
hence is shifted to larger distances. Representative snapshots indicate the discussed arrangements; hydrophilic and hydrophobic groups are shown in red/grey and blue/yellow, respectively. (b) Phase diagram for the dimerization ability when changing the membrane anchor lengths 
and 
of a pair of PMPs. Color-coded values of 
indicate the binding strength. Please note the logarithmic scale of the color-coding; values with 
are marked in black.