Charge-Induced Patchy Attractions between Proteins

Weimin Li; Björn Persson; Maxim Morin; Manja Behrens; Mikael Lund; Malin Zackrisson Oskolkova

doi:10.1021/jp512027j

Charge-Induced Patchy Attractions between Proteins

Weimin Li, Björn Persson, Maxim Morin, Manja Behrens, Mikael Lund, Malin Zackrisson Oskolkova

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	503-508
Journal	The Journal of Physical Chemistry Part B
Volume	119
Issue number	2
DOIs	https://doi.org/10.1021/jp512027j
Publication status	Published - 2015

Bibliographical note

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)

Subject classification (UKÄ)

Physical Chemistry (including Surface- and Colloid Chemistry)
Theoretical Chemistry (including Computational Chemistry)

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10.1021/jp512027j

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title = "Charge-Induced Patchy Attractions between Proteins",

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 = "Weimin Li and Bj{\"o}rn Persson and Maxim Morin and Manja Behrens and Mikael Lund and {Zackrisson Oskolkova}, Malin",

note = "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)",

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language = "English",

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pages = "503--508",

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T1 - Charge-Induced Patchy Attractions between Proteins

AU - Li, Weimin

AU - Persson, Björn

AU - Morin, Maxim

AU - Behrens, Manja

AU - Lund, Mikael

AU - Zackrisson Oskolkova, Malin

N1 - 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)

PY - 2015

Y1 - 2015

N2 - 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.

AB - 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.

U2 - 10.1021/jp512027j

DO - 10.1021/jp512027j

M3 - Article

C2 - 25494398

SN - 1520-5207

VL - 119

SP - 503

EP - 508

JO - The Journal of Physical Chemistry Part B

JF - The Journal of Physical Chemistry Part B

IS - 2

ER -

Charge-Induced Patchy Attractions between Proteins

Abstract

Bibliographical note

Subject classification (UKÄ)

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