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Charge-Induced Patchy Attractions between Proteins

Li, Weimin LU ; Persson, Björn LU ; Morin, Maxim LU ; Behrens, Manja LU ; Lund, Mikael LU and Zackrisson Oskolkova, Malin LU (2015) In The Journal of Physical Chemistry Part B 119(2). p.503-508
Abstract
Static light scattering (SLS) combined with structure-based Monte Carlo (MC) simulations provide new insights into mechanisms behind anisotropic, attractive protein interactions. A nonmonotonic behavior of the osmotic second virial coefficient as a function of ionic strength is here shown to originate from a few charged amino acids forming an electrostatic attractive patch, highly directional and complementary. Together with Coulombic repulsion, this attractive patch results in two counteracting electrostatic contributions to the interaction free energy which, by operating over different length scales, is manifested in a subtle, salt-induced minimum in the second virial coefficient as observed in both experiment and simulations.
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author
; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
The Journal of Physical Chemistry Part B
volume
119
issue
2
pages
503 - 508
publisher
The American Chemical Society (ACS)
external identifiers
  • wos:000348093700012
  • scopus:84921367899
  • pmid:25494398
ISSN
1520-5207
DOI
10.1021/jp512027j
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), Physical Chemistry 1 (S) (011001006)
id
84434d9c-6d67-448c-814f-fa93bc7b9ffd (old id 5178971)
date added to LUP
2016-04-01 12:57:23
date last changed
2020-09-23 03:01:37
@article{84434d9c-6d67-448c-814f-fa93bc7b9ffd,
  abstract     = {Static light scattering (SLS) combined with structure-based Monte Carlo (MC) simulations provide new insights into mechanisms behind anisotropic, attractive protein interactions. A nonmonotonic behavior of the osmotic second virial coefficient as a function of ionic strength is here shown to originate from a few charged amino acids forming an electrostatic attractive patch, highly directional and complementary. Together with Coulombic repulsion, this attractive patch results in two counteracting electrostatic contributions to the interaction free energy which, by operating over different length scales, is manifested in a subtle, salt-induced minimum in the second virial coefficient as observed in both experiment and simulations.},
  author       = {Li, Weimin and Persson, Björn and Morin, Maxim and Behrens, Manja and Lund, Mikael and Zackrisson Oskolkova, Malin},
  issn         = {1520-5207},
  language     = {eng},
  number       = {2},
  pages        = {503--508},
  publisher    = {The American Chemical Society (ACS)},
  series       = {The Journal of Physical Chemistry Part B},
  title        = {Charge-Induced Patchy Attractions between Proteins},
  url          = {http://dx.doi.org/10.1021/jp512027j},
  doi          = {10.1021/jp512027j},
  volume       = {119},
  year         = {2015},
}