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Anisotropic protein-protein interactions due to ion binding.

Lund, Mikael LU (2016) In Colloids and Surfaces B: Biointerfaces 137(Online 19 June 2015). p.17-21
Abstract
Self-association of proteins is strongly affected by long-range electrostatic interactions caused by equilibrium adsorption of small ions such as protons and multivalent metals. By affecting the molecular net charge, solution pH is thus a widely used parameter to tune stability and phase behavior of proteins. We here review recent studies where the charge distribution is perturbed not only by protons, but also by other binding ions, leading to a rich and inherently anisotropic charge distribution. Focus is on coarse grained simulation techniques, coupled to experiments of protein-protein interaction at varying salt and pH conditions. Finally, and with future bio-colloidal models in mind, we discuss the validity of coarse graining charge... (More)
Self-association of proteins is strongly affected by long-range electrostatic interactions caused by equilibrium adsorption of small ions such as protons and multivalent metals. By affecting the molecular net charge, solution pH is thus a widely used parameter to tune stability and phase behavior of proteins. We here review recent studies where the charge distribution is perturbed not only by protons, but also by other binding ions, leading to a rich and inherently anisotropic charge distribution. Focus is on coarse grained simulation techniques, coupled to experiments of protein-protein interaction at varying salt and pH conditions. Finally, and with future bio-colloidal models in mind, we discuss the validity of coarse graining charge anisotropy using electric multipoles. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Colloids and Surfaces B: Biointerfaces
volume
137
issue
Online 19 June 2015
pages
17 - 21
publisher
Elsevier
external identifiers
  • pmid:26162300
  • wos:000367491200003
  • scopus:84951574080
ISSN
1873-4367
DOI
10.1016/j.colsurfb.2015.05.054
language
English
LU publication?
yes
id
aa9d62e4-1ae5-415a-8b51-d9f82fd27a74 (old id 7749916)
date added to LUP
2015-09-24 17:47:14
date last changed
2017-08-27 03:34:38
@article{aa9d62e4-1ae5-415a-8b51-d9f82fd27a74,
  abstract     = {Self-association of proteins is strongly affected by long-range electrostatic interactions caused by equilibrium adsorption of small ions such as protons and multivalent metals. By affecting the molecular net charge, solution pH is thus a widely used parameter to tune stability and phase behavior of proteins. We here review recent studies where the charge distribution is perturbed not only by protons, but also by other binding ions, leading to a rich and inherently anisotropic charge distribution. Focus is on coarse grained simulation techniques, coupled to experiments of protein-protein interaction at varying salt and pH conditions. Finally, and with future bio-colloidal models in mind, we discuss the validity of coarse graining charge anisotropy using electric multipoles.},
  author       = {Lund, Mikael},
  issn         = {1873-4367},
  language     = {eng},
  number       = {Online 19 June 2015},
  pages        = {17--21},
  publisher    = {Elsevier},
  series       = {Colloids and Surfaces B: Biointerfaces},
  title        = {Anisotropic protein-protein interactions due to ion binding.},
  url          = {http://dx.doi.org/10.1016/j.colsurfb.2015.05.054},
  volume       = {137},
  year         = {2016},
}