title: Charge-induced patchy attractions between proteins.
abstract: Static light scattering (SLS) combined with structure-based Monte Carlo (MC) simulations provide new insights into mechanisms behind anisotropic, attractive protein interactions. A nonmonotonic behavior of the osmotic second virial coefficient as a function of ionic strength is here shown to originate from a few charged amino acids forming an electrostatic attractive patch, highly directional and complementary. Together with Coulombic repulsion, this attractive patch results in two counteracting electrostatic contributions to the interaction free energy which, by operating over different length scales, is manifested in a subtle, salt-induced minimum in the second virial coefficient as observed in both experiment and simulations.
authors.affiliation: Division of Physical Chemistry and ‡Division of Theoretical Chemistry, Lund University , POB 124, 22100 Lund, Sweden.
authors.forename: Weimin
authors.initials: W
authors.lastname: Li
authors.forename: Björn A
authors.initials: BA
authors.lastname: Persson
authors.forename: Maxim
authors.initials: M
authors.lastname: Morin
authors.forename: Manja A
authors.initials: MA
authors.lastname: Behrens
authors.forename: Mikael
authors.initials: M
authors.lastname: Lund
authors.forename: Malin
authors.initials: M
authors.lastname: Zackrisson Oskolkova
mesh_terms: D008958:Models, Molecular; D009010:Monte Carlo Method; D009994:Osmolar Concentration; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D055672:Static Electricity
chemical_list: D011506:Proteins