Molecular evidence of stereo-specific lactoferrin dimers in solution.
Persson, Björn LU ; Lund, Mikael LU
; Forsman, Jan
LU
; Chatterton, Dereck E W
and Åkesson, Torbjörn
LU
(2010)
In Biophysical Chemistry
151(3).
p.187-189
- Abstract
- Gathering experimental evidence suggests that bovine as well as human lactoferrin self-associate in aqueous solution. Still, a molecular level explanation is unavailable. Using force field based molecular modeling of the protein-protein interaction free energy we demonstrate (1) that lactoferrin forms highly stereo-specific dimers at neutral pH and (2) that the self-association is driven by a high charge complementarity across the contact surface of the proteins. Our theoretical predictions of dimer formation are verified by electrophoretic mobility and N-terminal sequence analysis on bovine lactoferrin.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1665732
- author
- Persson, Björn
LU
; Lund, Mikael
LU
; Forsman, Jan
LU
; Chatterton, Dereck E W
and Åkesson, Torbjörn
LU
- organization
- publishing date
- 2010
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biophysical Chemistry
- volume
- 151
- issue
- 3
- pages
- 187 - 189
- publisher
- Elsevier
- external identifiers
-
- wos:000281920700013
- pmid:20674143
- scopus:77955846507
- pmid:20674143
- ISSN
- 1873-4200
- DOI
- 10.1016/j.bpc.2010.06.005
- 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
- b6f094c7-4785-468a-b133-4faf7acc74df (old id 1665732)
- date added to LUP
- 2016-04-01 13:10:40
- date last changed
- 2023-01-03 21:30:44
@article{b6f094c7-4785-468a-b133-4faf7acc74df,
abstract = {{Gathering experimental evidence suggests that bovine as well as human lactoferrin self-associate in aqueous solution. Still, a molecular level explanation is unavailable. Using force field based molecular modeling of the protein-protein interaction free energy we demonstrate (1) that lactoferrin forms highly stereo-specific dimers at neutral pH and (2) that the self-association is driven by a high charge complementarity across the contact surface of the proteins. Our theoretical predictions of dimer formation are verified by electrophoretic mobility and N-terminal sequence analysis on bovine lactoferrin.}},
author = {{Persson, Björn and Lund, Mikael and Forsman, Jan and Chatterton, Dereck E W and Åkesson, Torbjörn}},
issn = {{1873-4200}},
language = {{eng}},
number = {{3}},
pages = {{187--189}},
publisher = {{Elsevier}},
series = {{Biophysical Chemistry}},
title = {{Molecular evidence of stereo-specific lactoferrin dimers in solution.}},
url = {{http://dx.doi.org/10.1016/j.bpc.2010.06.005}},
doi = {{10.1016/j.bpc.2010.06.005}},
volume = {{151}},
year = {{2010}},
}