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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/5178971
- author
- Li, Weimin
LU
; Persson, Björn
LU
; Morin, Maxim
LU
; Behrens, Manja
LU
; Lund, Mikael
LU
and Zackrisson Oskolkova, Malin
LU
- organization
- publishing date
- 2015
- 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
- 2023-04-05 21:43:46
@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}},
}