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Photo Mikael Lund

Mikael Lund

Professor

Photo Mikael Lund

Anisotropic Interactions in Protein Mixtures,: Self Assembly and Phase Behavior in Aqueous Solution

Author

  • Anil Kurut Sabanoglu
  • Björn Persson
  • Torbjörn Åkesson
  • Jan Forsman
  • Mikael Lund

Summary, in English

Recent experimental studies show that oppositely charged proteins can self-assemble to form seemingly stable microspheres in aqueous salt solutions. We here use parallel tempering Monte Carlo simulations to study protein phase separation of lysozyme/alpha-lactalbumin mixtures and show that anisotropic electrostatic interactions are important for driving protein self-assembly. In both dilute and concentrated protein phases, the proteins strongly align according to their charge distribution. While this alignment can be greatly diminished by a single point mutation, phase separation is completely suppressed when neglecting electrostatic anisotropy. The results highlight the importance of subtle electrostatic interactions even in crowded biomolecular environments where other short-ranged forces are often thought to dominate.

Department/s

  • Computational Chemistry
  • eSSENCE: The e-Science Collaboration

Publishing year

2012

Language

English

Pages

731-734

Publication/Series

The Journal of Physical Chemistry Letters

Volume

3

Issue

6

Document type

Journal article

Publisher

The American Chemical Society (ACS)

Topic

  • Theoretical Chemistry (including Computational Chemistry)

Status

Published

ISBN/ISSN/Other

  • ISSN: 1948-7185