Enhanced Protein Steering: Cooperative Electrostatic and van der Waals Forces in Antigen-Antibody Complexes.
(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:
https://lup.lub.lu.se/record/1453337
- author
- Persson, Björn LU ; Jönsson, Bo LU and Lund, Mikael LU
- organization
- publishing date
- 2009
- 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
- 2023-01-03 22:24:44
@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}}, }