Advanced

Effect of spatially distributed hydrophobic surface residues on protein-polymer association

Jönsson, Malin LU ; Skepö, Marie LU ; Tjerneld, Folke LU and Linse, Per LU (2003) In The Journal of Physical Chemistry Part B 107(23). p.5511-5518
Abstract
The effect of the spatial distribution of hydrophobic surface residues on the adsorption of a weakly hydrophobic polymer to proteins has been examined using a coarse-grain model solved by Monte Carlo simulations. A given number of surface sites were distributed randomly on the protein surface subjected to a distance constraint. Five protein classes for which the minimum distance between the sites was 2, 3, 4, 5, and 6 Angstrom were considered, and for each class 10 proteins with different site distributions randomly generated were examined. As the strength of the hydrophobic interaction was increased, the onset of the polymer adsorption to the protein appeared first for proteins with a more heterogeneous site distribution. This holds both... (More)
The effect of the spatial distribution of hydrophobic surface residues on the adsorption of a weakly hydrophobic polymer to proteins has been examined using a coarse-grain model solved by Monte Carlo simulations. A given number of surface sites were distributed randomly on the protein surface subjected to a distance constraint. Five protein classes for which the minimum distance between the sites was 2, 3, 4, 5, and 6 Angstrom were considered, and for each class 10 proteins with different site distributions randomly generated were examined. As the strength of the hydrophobic interaction was increased, the onset of the polymer adsorption to the protein appeared first for proteins with a more heterogeneous site distribution. This holds both for the systematic variation of the site distribution for protein

of different classes and for the random variation among proteins within a class. The degree of heterogeneity of the site distributions was quantified using the variance of the number of sites located within randomly positioned circles placed on the protein surface. The conformational changes of the polymer at the adsorption were also studied. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
The Journal of Physical Chemistry Part B
volume
107
issue
23
pages
5511 - 5518
publisher
The American Chemical Society
external identifiers
  • wos:000183403700018
  • scopus:0038681862
ISSN
1520-5207
DOI
10.1021/jp0223253
language
English
LU publication?
yes
id
840a0ab6-4fbc-4654-920c-1c5e852de1eb (old id 122026)
date added to LUP
2007-07-05 16:47:06
date last changed
2017-05-21 04:30:15
@article{840a0ab6-4fbc-4654-920c-1c5e852de1eb,
  abstract     = {The effect of the spatial distribution of hydrophobic surface residues on the adsorption of a weakly hydrophobic polymer to proteins has been examined using a coarse-grain model solved by Monte Carlo simulations. A given number of surface sites were distributed randomly on the protein surface subjected to a distance constraint. Five protein classes for which the minimum distance between the sites was 2, 3, 4, 5, and 6 Angstrom were considered, and for each class 10 proteins with different site distributions randomly generated were examined. As the strength of the hydrophobic interaction was increased, the onset of the polymer adsorption to the protein appeared first for proteins with a more heterogeneous site distribution. This holds both for the systematic variation of the site distribution for protein<br/><br>
 of different classes and for the random variation among proteins within a class. The degree of heterogeneity of the site distributions was quantified using the variance of the number of sites located within randomly positioned circles placed on the protein surface. The conformational changes of the polymer at the adsorption were also studied.},
  author       = {Jönsson, Malin and Skepö, Marie and Tjerneld, Folke and Linse, Per},
  issn         = {1520-5207},
  language     = {eng},
  number       = {23},
  pages        = {5511--5518},
  publisher    = {The American Chemical Society},
  series       = {The Journal of Physical Chemistry Part B},
  title        = {Effect of spatially distributed hydrophobic surface residues on protein-polymer association},
  url          = {http://dx.doi.org/10.1021/jp0223253},
  volume       = {107},
  year         = {2003},
}