How the excluded volume architecture influences ion-mediated forces between proteins.
The effective interactions between model proteins of various shapes are computed by means of Monte Carlo simulations. In particular, we determine how the modification of the excluded volume architecture influences both entropic and purely electrostatic ion-mediated forces between proteins. We find that interprotein interactions are strongly affected by protein shape, which results in a high decrease of electrostatic screening for typical active site geometries. Effective interactions are then closer to the direct Coulombic interactions, and both affinity and selectivity are enhanced by several orders of magnitude.
Dahirel
V
V
Laboratoire Liquides Ioniques et Interfaces Chargées, UMR CNRS 7612, Université Pierre et Marie Curie-Paris 6, case courrier 51, 4 place Jussieu F-75252, Paris Cedex 05, France.
Jardat
M
M
Dufrêche
J-F
JF
Turq
P
P
D000818:Animals; D000838:Anions; D001703:Biophysics / Q000379:methods*; D019277:Entropy; D006801:Humans; D007477:Ions; D008954:Models, Biological; D015233:Models, Statistical; D008962:Models, Theoretical; D009010:Monte Carlo Method; D025941:Protein Interaction Mapping; D011506:Proteins / Q000737:chemistry*; D055672:Static Electricity; D013816:Thermodynamics
D000838:Anions; D007477:Ions; D011506:Proteins