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Structure and thermodynamics of protein-polymer solutions: Effects of spatially distributed hydrophobic surface residues

Jönsson, Malin LU and Linse, Per LU (2005) In The Journal of Physical Chemistry Part B 109(31). p.15107-15117
Abstract
Protein-polymer association in solution driven by a short-range attraction has been investigated using a simple coarse-grain model solved by Monte Carlo simulations. The effect of the spatial distribution of the hydrophobic surface residues of the protein on the adsorption of weakly hydrophobic polymers at variable polymer concentration, polymer length, and polymer stiffness has been considered. Structural data on the adsorbed polymer layer and thermodynamic properties, such as the free energy, energy, and entropy, related to the protein-polymer interaction were calculated. It was found that a more heterogeneous distribution of the surface residues promotes adsorption and that this also applies for different polymer concentrations, polymer... (More)
Protein-polymer association in solution driven by a short-range attraction has been investigated using a simple coarse-grain model solved by Monte Carlo simulations. The effect of the spatial distribution of the hydrophobic surface residues of the protein on the adsorption of weakly hydrophobic polymers at variable polymer concentration, polymer length, and polymer stiffness has been considered. Structural data on the adsorbed polymer layer and thermodynamic properties, such as the free energy, energy, and entropy, related to the protein-polymer interaction were calculated. It was found that a more heterogeneous distribution of the surface residues promotes adsorption and that this also applies for different polymer concentrations, polymer chain lengths, and polymer flexibilities. Furthermore, the polymer adsorption onto proteins with more homogeneous surface distributions displayed larger sensitivity to polymer properties such as chain length and flexibility. Finally, a simple relation between the adsorption probability and the change in the free energy was found and rationalized by a simple two-state adsorption model. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
The Journal of Physical Chemistry Part B
volume
109
issue
31
pages
15107 - 15117
publisher
The American Chemical Society
external identifiers
  • wos:000231042800050
  • scopus:23844449777
ISSN
1520-5207
DOI
10.1021/jp0451288
language
English
LU publication?
yes
id
57e56e20-81d4-4208-b88a-791583cdd911 (old id 157410)
date added to LUP
2007-07-11 13:37:35
date last changed
2017-03-05 04:05:15
@article{57e56e20-81d4-4208-b88a-791583cdd911,
  abstract     = {Protein-polymer association in solution driven by a short-range attraction has been investigated using a simple coarse-grain model solved by Monte Carlo simulations. The effect of the spatial distribution of the hydrophobic surface residues of the protein on the adsorption of weakly hydrophobic polymers at variable polymer concentration, polymer length, and polymer stiffness has been considered. Structural data on the adsorbed polymer layer and thermodynamic properties, such as the free energy, energy, and entropy, related to the protein-polymer interaction were calculated. It was found that a more heterogeneous distribution of the surface residues promotes adsorption and that this also applies for different polymer concentrations, polymer chain lengths, and polymer flexibilities. Furthermore, the polymer adsorption onto proteins with more homogeneous surface distributions displayed larger sensitivity to polymer properties such as chain length and flexibility. Finally, a simple relation between the adsorption probability and the change in the free energy was found and rationalized by a simple two-state adsorption model.},
  author       = {Jönsson, Malin and Linse, Per},
  issn         = {1520-5207},
  language     = {eng},
  number       = {31},
  pages        = {15107--15117},
  publisher    = {The American Chemical Society},
  series       = {The Journal of Physical Chemistry Part B},
  title        = {Structure and thermodynamics of protein-polymer solutions: Effects of spatially distributed hydrophobic surface residues},
  url          = {http://dx.doi.org/10.1021/jp0451288},
  volume       = {109},
  year         = {2005},
}