Abstract
Numerical simulations of hydrated proteins show that protein hydration shells are polarized into a ferroelectric layer with large values of the average dipole moment magnitude and the dipole moment variance. The emergence of the new polarized mesophase dramatically alters the statistics of electrostatic fluctuations at the protein-water interface. The linear response relation between the average electrostatic potential and its variance breaks down, with the breadth of the electrostatic fluctuations far exceeding the expectations of the linear response theories. The dynamics of these non-Gaussian electrostatic fluctuations are dominated by a slow (≲1 ns) component that freezes in at the temperature of the dynamical transition of proteins. The ferroelectric shell propagates 3-5 water diameters into the bulk.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 9246-9258 |
| Number of pages | 13 |
| Journal | Journal of Physical Chemistry B |
| Volume | 114 |
| Issue number | 28 |
| DOIs | |
| State | Published - Jul 22 2010 |
Fingerprint
ASJC Scopus subject areas
- Physical and Theoretical Chemistry
- Materials Chemistry
- Surfaces, Coatings and Films
Cite this
Ferroelectric hydration shells around proteins : Electrostatics of the protein-water interface. / Lebard, David N.; Matyushov, Dmitry.
In: Journal of Physical Chemistry B, Vol. 114, No. 28, 22.07.2010, p. 9246-9258.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Ferroelectric hydration shells around proteins
T2 - Electrostatics of the protein-water interface
AU - Lebard, David N.
AU - Matyushov, Dmitry
PY - 2010/7/22
Y1 - 2010/7/22
N2 - Numerical simulations of hydrated proteins show that protein hydration shells are polarized into a ferroelectric layer with large values of the average dipole moment magnitude and the dipole moment variance. The emergence of the new polarized mesophase dramatically alters the statistics of electrostatic fluctuations at the protein-water interface. The linear response relation between the average electrostatic potential and its variance breaks down, with the breadth of the electrostatic fluctuations far exceeding the expectations of the linear response theories. The dynamics of these non-Gaussian electrostatic fluctuations are dominated by a slow (≲1 ns) component that freezes in at the temperature of the dynamical transition of proteins. The ferroelectric shell propagates 3-5 water diameters into the bulk.
AB - Numerical simulations of hydrated proteins show that protein hydration shells are polarized into a ferroelectric layer with large values of the average dipole moment magnitude and the dipole moment variance. The emergence of the new polarized mesophase dramatically alters the statistics of electrostatic fluctuations at the protein-water interface. The linear response relation between the average electrostatic potential and its variance breaks down, with the breadth of the electrostatic fluctuations far exceeding the expectations of the linear response theories. The dynamics of these non-Gaussian electrostatic fluctuations are dominated by a slow (≲1 ns) component that freezes in at the temperature of the dynamical transition of proteins. The ferroelectric shell propagates 3-5 water diameters into the bulk.
UR - http://www.scopus.com/inward/record.url?scp=77954715967&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=77954715967&partnerID=8YFLogxK
U2 - 10.1021/jp1006999
DO - 10.1021/jp1006999
M3 - Article
C2 - 20578769
AN - SCOPUS:77954715967
VL - 114
SP - 9246
EP - 9258
JO - Journal of Physical Chemistry B Materials
JF - Journal of Physical Chemistry B Materials
SN - 1520-6106
IS - 28
ER -