On the charge regulation of proteins
(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:
https://lup.lub.lu.se/record/152763
- author
- Lund, Mikael LU and Jönsson, Bo LU
- organization
- publishing date
- 2005
- 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}}, }