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Enhanced Protein Steering: Cooperative Electrostatic and van der Waals Forces in Antigen-Antibody Complexes.

Persson, Björn LU ; Jönsson, Bo LU and Lund, Mikael LU orcid (2009) In The Journal of Physical Chemistry Part B 113(30). p.10459-10464
Abstract
We study the association of the cationic protein lysozyme with several almost neutral protein fragments but with highly uneven charge distributions. Using mesoscopic protein models, we show how electrostatic interactions can align or steer protein complexes into specific constellations dictated by the specific charge distributions of the interacting biomolecules. Including van der Waals forces significantly amplifies the electrostatically induced orientational steering at physiological solution conditions, demonstrating that different intermolecular interactions can work in a cooperative way in order to optimize specific biochemical mechanisms. Individually, the electrostatic and van der Waals interactions lead only to a relatively weak... (More)
We study the association of the cationic protein lysozyme with several almost neutral protein fragments but with highly uneven charge distributions. Using mesoscopic protein models, we show how electrostatic interactions can align or steer protein complexes into specific constellations dictated by the specific charge distributions of the interacting biomolecules. Including van der Waals forces significantly amplifies the electrostatically induced orientational steering at physiological solution conditions, demonstrating that different intermolecular interactions can work in a cooperative way in order to optimize specific biochemical mechanisms. Individually, the electrostatic and van der Waals interactions lead only to a relatively weak intermolecular alignment, but when combined, the effect increases significantly. (Less)
Please use this url to cite or link to this publication:
author
; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
The Journal of Physical Chemistry Part B
volume
113
issue
30
pages
10459 - 10464
publisher
The American Chemical Society (ACS)
external identifiers
  • wos:000268231000055
  • pmid:19583233
  • scopus:67651207529
  • pmid:19583233
ISSN
1520-5207
DOI
10.1021/jp904541g
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
e63ebffd-f91a-4532-8a3b-45d93c0746bf (old id 1453337)
date added to LUP
2016-04-01 13:20:21
date last changed
2021-09-15 05:12:11
@article{e63ebffd-f91a-4532-8a3b-45d93c0746bf,
  abstract     = {We study the association of the cationic protein lysozyme with several almost neutral protein fragments but with highly uneven charge distributions. Using mesoscopic protein models, we show how electrostatic interactions can align or steer protein complexes into specific constellations dictated by the specific charge distributions of the interacting biomolecules. Including van der Waals forces significantly amplifies the electrostatically induced orientational steering at physiological solution conditions, demonstrating that different intermolecular interactions can work in a cooperative way in order to optimize specific biochemical mechanisms. Individually, the electrostatic and van der Waals interactions lead only to a relatively weak intermolecular alignment, but when combined, the effect increases significantly.},
  author       = {Persson, Björn and Jönsson, Bo and Lund, Mikael},
  issn         = {1520-5207},
  language     = {eng},
  number       = {30},
  pages        = {10459--10464},
  publisher    = {The American Chemical Society (ACS)},
  series       = {The Journal of Physical Chemistry Part B},
  title        = {Enhanced Protein Steering: Cooperative Electrostatic and van der Waals Forces in Antigen-Antibody Complexes.},
  url          = {http://dx.doi.org/10.1021/jp904541g},
  doi          = {10.1021/jp904541g},
  volume       = {113},
  year         = {2009},
}