Advanced

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

Kurut Sabanoglu, Anil LU ; Persson, Björn LU ; Åkesson, Torbjörn LU ; Forsman, Jan LU and Lund, Mikael LU (2012) In The Journal of Physical Chemistry Letters 3(6). p.731-734
Abstract
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... (More)
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. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
The Journal of Physical Chemistry Letters
volume
3
issue
6
pages
731 - 734
publisher
The American Chemical Society
external identifiers
  • wos:000301629000011
  • scopus:84858665589
ISSN
1948-7185
DOI
10.1021/jz201680m
language
English
LU publication?
yes
id
f57c06c6-6351-4cda-81a7-8342bb8f39ee (old id 2515525)
date added to LUP
2012-05-09 14:55:00
date last changed
2017-11-05 04:05:38
@article{f57c06c6-6351-4cda-81a7-8342bb8f39ee,
  abstract     = {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.},
  author       = {Kurut Sabanoglu, Anil and Persson, Björn and Åkesson, Torbjörn and Forsman, Jan and Lund, Mikael},
  issn         = {1948-7185},
  language     = {eng},
  number       = {6},
  pages        = {731--734},
  publisher    = {The American Chemical Society},
  series       = {The Journal of Physical Chemistry Letters},
  title        = {Anisotropic Interactions in Protein Mixtures,: Self Assembly and Phase Behavior in Aqueous Solution},
  url          = {http://dx.doi.org/10.1021/jz201680m},
  volume       = {3},
  year         = {2012},
}