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Protein-polyelectrolyte cluster formatio and redissolution: A Monte Carlo study

Carlsson, F; Malmsten, M and Linse, Per LU (2003) In Journal of the American Chemical Society 125(10). p.3140-3149
Abstract
Aqueous solutions of proteins and oppositely charged polyelectrolytes were studied at different polyelectrolyte chain length, ionic strength, and protein-protein interaction potential as a function of the polyelectrolyte concentration. One of the protein models used represented lysozyme in aqueous environment. The model systems were solved by Monte Carlo simulations, and their properties were analyzed in terms of radial distribution functions, structure factors, and cluster composition probabilities. In the system with the strongest electrostatic protein-polyelectrolyte interaction the largest clusters were formed near or at equivalent amount of net protein charge and polyelectrolyte charge, whereas in excess of polyelectrolyte a... (More)
Aqueous solutions of proteins and oppositely charged polyelectrolytes were studied at different polyelectrolyte chain length, ionic strength, and protein-protein interaction potential as a function of the polyelectrolyte concentration. One of the protein models used represented lysozyme in aqueous environment. The model systems were solved by Monte Carlo simulations, and their properties were analyzed in terms of radial distribution functions, structure factors, and cluster composition probabilities. In the system with the strongest electrostatic protein-polyelectrolyte interaction the largest clusters were formed near or at equivalent amount of net protein charge and polyelectrolyte charge, whereas in excess of polyelectrolyte a redissolution appeared. Shorter polyelectrolyte chains and increased ionic strength lead to weaker cluster formation. An inclusion of nonelectrostatic

protein-protein attraction promoted the protein-polyelectrolyte cluster

formation. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of the American Chemical Society
volume
125
issue
10
pages
3140 - 3149
publisher
The American Chemical Society
external identifiers
  • wos:000181409500062
  • pmid:12617682
  • scopus:0037433601
ISSN
1520-5126
DOI
10.1021/ja020935a
language
English
LU publication?
yes
id
2acc3245-85f6-48a0-81bd-2cf2a71f85d7 (old id 121960)
date added to LUP
2007-07-11 08:52:10
date last changed
2017-08-06 04:36:34
@article{2acc3245-85f6-48a0-81bd-2cf2a71f85d7,
  abstract     = {Aqueous solutions of proteins and oppositely charged polyelectrolytes were studied at different polyelectrolyte chain length, ionic strength, and protein-protein interaction potential as a function of the polyelectrolyte concentration. One of the protein models used represented lysozyme in aqueous environment. The model systems were solved by Monte Carlo simulations, and their properties were analyzed in terms of radial distribution functions, structure factors, and cluster composition probabilities. In the system with the strongest electrostatic protein-polyelectrolyte interaction the largest clusters were formed near or at equivalent amount of net protein charge and polyelectrolyte charge, whereas in excess of polyelectrolyte a redissolution appeared. Shorter polyelectrolyte chains and increased ionic strength lead to weaker cluster formation. An inclusion of nonelectrostatic<br/><br>
protein-protein attraction promoted the protein-polyelectrolyte cluster<br/><br>
	formation.},
  author       = {Carlsson, F and Malmsten, M and Linse, Per},
  issn         = {1520-5126},
  language     = {eng},
  number       = {10},
  pages        = {3140--3149},
  publisher    = {The American Chemical Society},
  series       = {Journal of the American Chemical Society},
  title        = {Protein-polyelectrolyte cluster formatio and redissolution: A Monte Carlo study},
  url          = {http://dx.doi.org/10.1021/ja020935a},
  volume       = {125},
  year         = {2003},
}