Fast Proton Titration Scheme for Multiscale Modeling of Protein Solutions
Reis Teixeira, Andre Azevedo ; Lund, Mikael LU
and Barroso da Silva, Fernando Luis
(2010)
In Journal of Chemical Theory and Computation
6(10).
p.3259-3266
- Abstract
- Proton exchange between titratable amino acid residues and the surrounding solution gives rise to exciting electric processes in proteins. We present a proton titration scheme for studying acid-base equilibria in Metropolis Monte Carlo simulations where salt is treated at the Debye-Huckel level. The method, rooted in the Kirkwood model of impenetrable spheres, is applied on the three milk proteins alpha-lactalbumin, beta-lactoglobulin, and lactoferrin, for which we investigate the net-charge, molecular dipole moment, and charge capacitance. Over a wide range of pH and salt conditions, excellent agreement is found with more elaborate simulations where salt is explicitly included. The implicit salt scheme is orders of magnitude faster than... (More)
- Proton exchange between titratable amino acid residues and the surrounding solution gives rise to exciting electric processes in proteins. We present a proton titration scheme for studying acid-base equilibria in Metropolis Monte Carlo simulations where salt is treated at the Debye-Huckel level. The method, rooted in the Kirkwood model of impenetrable spheres, is applied on the three milk proteins alpha-lactalbumin, beta-lactoglobulin, and lactoferrin, for which we investigate the net-charge, molecular dipole moment, and charge capacitance. Over a wide range of pH and salt conditions, excellent agreement is found with more elaborate simulations where salt is explicitly included. The implicit salt scheme is orders of magnitude faster than the explicit analog and allows for transparent interpretation of physical mechanisms. It is shown how the method can be expanded to multiscale modeling of aqueous salt solutions of many biomolecules with nonstatic charge distributions. Important examples are protein-protein aggregation, protein-polyelectrolyte complexation, and protein-membrane association. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1726064
- author
- Reis Teixeira, Andre Azevedo
; Lund, Mikael
LU
and Barroso da Silva, Fernando Luis
- organization
- publishing date
- 2010
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Chemical Theory and Computation
- volume
- 6
- issue
- 10
- pages
- 3259 - 3266
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- wos:000282840600027
- scopus:77957946626
- pmid:26616787
- ISSN
- 1549-9618
- DOI
- 10.1021/ct1003093
- 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
- df02cb48-69e8-4e24-afd9-d50dedd82be8 (old id 1726064)
- date added to LUP
- 2016-04-01 10:35:26
- date last changed
- 2023-01-02 06:04:09
@article{df02cb48-69e8-4e24-afd9-d50dedd82be8,
abstract = {{Proton exchange between titratable amino acid residues and the surrounding solution gives rise to exciting electric processes in proteins. We present a proton titration scheme for studying acid-base equilibria in Metropolis Monte Carlo simulations where salt is treated at the Debye-Huckel level. The method, rooted in the Kirkwood model of impenetrable spheres, is applied on the three milk proteins alpha-lactalbumin, beta-lactoglobulin, and lactoferrin, for which we investigate the net-charge, molecular dipole moment, and charge capacitance. Over a wide range of pH and salt conditions, excellent agreement is found with more elaborate simulations where salt is explicitly included. The implicit salt scheme is orders of magnitude faster than the explicit analog and allows for transparent interpretation of physical mechanisms. It is shown how the method can be expanded to multiscale modeling of aqueous salt solutions of many biomolecules with nonstatic charge distributions. Important examples are protein-protein aggregation, protein-polyelectrolyte complexation, and protein-membrane association.}},
author = {{Reis Teixeira, Andre Azevedo and Lund, Mikael and Barroso da Silva, Fernando Luis}},
issn = {{1549-9618}},
language = {{eng}},
number = {{10}},
pages = {{3259--3266}},
publisher = {{The American Chemical Society (ACS)}},
series = {{Journal of Chemical Theory and Computation}},
title = {{Fast Proton Titration Scheme for Multiscale Modeling of Protein Solutions}},
url = {{http://dx.doi.org/10.1021/ct1003093}},
doi = {{10.1021/ct1003093}},
volume = {{6}},
year = {{2010}},
}