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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/7749916
- author
- Lund, Mikael
LU
- organization
- publishing date
- 2016
- 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
- pmid:26162300
- ISSN
- 1873-4367
- DOI
- 10.1016/j.colsurfb.2015.05.054
- 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
- aa9d62e4-1ae5-415a-8b51-d9f82fd27a74 (old id 7749916)
- date added to LUP
- 2016-04-01 10:46:52
- date last changed
- 2023-01-17 23:06:09
@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}},
doi = {{10.1016/j.colsurfb.2015.05.054}},
volume = {{137}},
year = {{2016}},
}