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On the charge regulation of proteins

Lund, Mikael LU orcid 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)
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author
and
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 (ACS)
external identifiers
  • pmid:15823030
  • wos:000228425600017
  • scopus:17144365075
  • pmid:15823030
ISSN
0006-2960
DOI
10.1021/bi047630o
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
93666e49-edf4-4038-86ad-b247d631364d (old id 152763)
date added to LUP
2016-04-01 11:46:41
date last changed
2023-03-26 08:13:42
@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 (ACS)}},
  series       = {{Biochemistry}},
  title        = {{On the charge regulation of proteins}},
  url          = {{http://dx.doi.org/10.1021/bi047630o}},
  doi          = {{10.1021/bi047630o}},
  volume       = {{44}},
  year         = {{2005}},
}