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On the charge regulation of proteins

Lund, Mikael LU and Jönsson, Bo LU (2005) In Biochemistry 44(15). p.5722-5727
Abstract
It is known that the overall charge of a protein can change as the molecule approaches a charged object like another protein or a cell membrane. We have formalized this mechanism using a statistical mechanical framework and show how this rather overlooked interaction increases the attraction between protein molecules. From the theory, we can identify a unique property, the protein charge capacitance, that contains all information needed to describe the charge regulation mechanism. The capacitance can be obtained from experiment or theory and is a function of pH, salt concentration, and the number of titrating residues. For a range of different protein molecules, we calculate the capacitance and demonstrate how it can be used to quantify... (More)
It is known that the overall charge of a protein can change as the molecule approaches a charged object like another protein or a cell membrane. We have formalized this mechanism using a statistical mechanical framework and show how this rather overlooked interaction increases the attraction between protein molecules. From the theory, we can identify a unique property, the protein charge capacitance, that contains all information needed to describe the charge regulation mechanism. The capacitance can be obtained from experiment or theory and is a function of pH, salt concentration, and the number of titrating residues. For a range of different protein molecules, we calculate the capacitance and demonstrate how it can be used to quantify the charge regulation interaction. With minimal effort, the derived formulas can be used to improve existing models by including a charge regulation term. Good agreement is found between theory, simulations, and experimental data. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochemistry
volume
44
issue
15
pages
5722 - 5727
publisher
The American Chemical Society
external identifiers
  • pmid:15823030
  • wos:000228425600017
  • scopus:17144365075
ISSN
0006-2960
DOI
10.1021/bi047630o
language
English
LU publication?
yes
id
93666e49-edf4-4038-86ad-b247d631364d (old id 152763)
date added to LUP
2007-07-17 11:53:45
date last changed
2017-11-05 03:31:58
@article{93666e49-edf4-4038-86ad-b247d631364d,
  abstract     = {It is known that the overall charge of a protein can change as the molecule approaches a charged object like another protein or a cell membrane. We have formalized this mechanism using a statistical mechanical framework and show how this rather overlooked interaction increases the attraction between protein molecules. From the theory, we can identify a unique property, the protein charge capacitance, that contains all information needed to describe the charge regulation mechanism. The capacitance can be obtained from experiment or theory and is a function of pH, salt concentration, and the number of titrating residues. For a range of different protein molecules, we calculate the capacitance and demonstrate how it can be used to quantify the charge regulation interaction. With minimal effort, the derived formulas can be used to improve existing models by including a charge regulation term. Good agreement is found between theory, simulations, and experimental data.},
  author       = {Lund, Mikael and Jönsson, Bo},
  issn         = {0006-2960},
  language     = {eng},
  number       = {15},
  pages        = {5722--5727},
  publisher    = {The American Chemical Society},
  series       = {Biochemistry},
  title        = {On the charge regulation of proteins},
  url          = {http://dx.doi.org/10.1021/bi047630o},
  volume       = {44},
  year         = {2005},
}