Charge-Induced Patchy Attractions between Proteins
2015-01-15
An article by scientists at the Division of Physical Chemistry is the ACS Editors' Choice in the Journal of Physical Chemistry.
The American Chemical Society (ACS) Editors have chosen the article to be published online and available through open access.
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.
Ref: "Charge-Induced Patchy Attractions between Proteins". Weimin Li †, Björn A. Persson ‡, Maxim Morin †, Manja A. Behrens †, Mikael Lund *‡, and Malin Zackrisson Oskolkova *†
†Division of Physical Chemistry and ‡Division of Theoretical Chemistry, Lund University