Anisotropic Interactions in Protein Mixtures,: Self Assembly and Phase Behavior in Aqueous Solution
(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:
https://lup.lub.lu.se/record/2515525
- author
- Kurut Sabanoglu, Anil LU ; Persson, Björn LU ; Åkesson, Torbjörn LU ; Forsman, Jan LU and Lund, Mikael LU
- organization
- publishing date
- 2012
- 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 (ACS)
- external identifiers
-
- wos:000301629000011
- scopus:84858665589
- ISSN
- 1948-7185
- DOI
- 10.1021/jz201680m
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Theoretical Chemistry (S) (011001039)
- id
- f57c06c6-6351-4cda-81a7-8342bb8f39ee (old id 2515525)
- date added to LUP
- 2016-04-01 14:04:12
- date last changed
- 2023-01-04 02:29:35
@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 (ACS)}}, series = {{The Journal of Physical Chemistry Letters}}, title = {{Anisotropic Interactions in Protein Mixtures,: Self Assembly and Phase Behavior in Aqueous Solution}}, url = {{https://lup.lub.lu.se/search/files/3761766/4053705.pdf}}, doi = {{10.1021/jz201680m}}, volume = {{3}}, year = {{2012}}, }