Concentration-Induced Association in a Protein System Caused by a Highly Directional Patch Attraction
Li, Weimin LU ; Persson, Björn A. LU ; Lund, Mikael LU
; Bergenholtz, Johan
and Zackrisson, Malin
LU
(2016)
In Journal of Physical Chemistry B
120(34).
p.8953-8959
- Abstract
Self-association of the protein lactoferrin is studied in solution using small-angle X-ray scattering techniques. Effective static structure factors have been shown to exhibit either a monotonic or a nonmonotonic dependence on protein concentration in the small wavevector limit, depending on salt concentration. The behavior correlates with a nonmonotonic dependence of the second virial coefficient on salt concentration, such that a maximum appears in the structure factor at a low protein concentration when the second virial coefficient is negative and close to a minimum. The results are interpreted in terms of an integral equation theory with explicit dimers, formulated by Wertheim, which provides a consistent framework able to explain... (More)
Self-association of the protein lactoferrin is studied in solution using small-angle X-ray scattering techniques. Effective static structure factors have been shown to exhibit either a monotonic or a nonmonotonic dependence on protein concentration in the small wavevector limit, depending on salt concentration. The behavior correlates with a nonmonotonic dependence of the second virial coefficient on salt concentration, such that a maximum appears in the structure factor at a low protein concentration when the second virial coefficient is negative and close to a minimum. The results are interpreted in terms of an integral equation theory with explicit dimers, formulated by Wertheim, which provides a consistent framework able to explain the behavior in terms of a monomer-dimer equilibrium that appears because of a highly directional patch attraction. Short attraction ranges preclude trimer formation, which explains why the protein system behaves as if it were subject to a concentration-dependent isotropic protein-protein attraction. Superimposing an isotropic interaction, comprising screened Coulomb repulsion and van der Waals attraction, on the patch attraction allows for a semiquantitative modeling of the complete transition pathway from monomers in the dilute limit to monomer-dimer systems at somewhat higher protein concentrations.
(Less)
- author
- Li, Weimin
LU
; Persson, Björn A.
LU
; Lund, Mikael
LU
; Bergenholtz, Johan
and Zackrisson, Malin
LU
- organization
- publishing date
- 2016-09-01
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Physical Chemistry B
- volume
- 120
- issue
- 34
- pages
- 7 pages
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- wos:000382596700021
- pmid:27447055
- scopus:84985955482
- ISSN
- 1520-6106
- DOI
- 10.1021/acs.jpcb.6b06873
- language
- English
- LU publication?
- yes
- id
- 19f47cd1-b846-43ea-b89a-c610b359495a
- date added to LUP
- 2016-11-11 15:34:53
- date last changed
- 2024-04-26 02:21:14
@article{19f47cd1-b846-43ea-b89a-c610b359495a,
abstract = {{<p>Self-association of the protein lactoferrin is studied in solution using small-angle X-ray scattering techniques. Effective static structure factors have been shown to exhibit either a monotonic or a nonmonotonic dependence on protein concentration in the small wavevector limit, depending on salt concentration. The behavior correlates with a nonmonotonic dependence of the second virial coefficient on salt concentration, such that a maximum appears in the structure factor at a low protein concentration when the second virial coefficient is negative and close to a minimum. The results are interpreted in terms of an integral equation theory with explicit dimers, formulated by Wertheim, which provides a consistent framework able to explain the behavior in terms of a monomer-dimer equilibrium that appears because of a highly directional patch attraction. Short attraction ranges preclude trimer formation, which explains why the protein system behaves as if it were subject to a concentration-dependent isotropic protein-protein attraction. Superimposing an isotropic interaction, comprising screened Coulomb repulsion and van der Waals attraction, on the patch attraction allows for a semiquantitative modeling of the complete transition pathway from monomers in the dilute limit to monomer-dimer systems at somewhat higher protein concentrations.</p>}},
author = {{Li, Weimin and Persson, Björn A. and Lund, Mikael and Bergenholtz, Johan and Zackrisson, Malin}},
issn = {{1520-6106}},
language = {{eng}},
month = {{09}},
number = {{34}},
pages = {{8953--8959}},
publisher = {{The American Chemical Society (ACS)}},
series = {{Journal of Physical Chemistry B}},
title = {{Concentration-Induced Association in a Protein System Caused by a Highly Directional Patch Attraction}},
url = {{http://dx.doi.org/10.1021/acs.jpcb.6b06873}},
doi = {{10.1021/acs.jpcb.6b06873}},
volume = {{120}},
year = {{2016}},
}