The role of electrostatic interactions in calmodulin-peptide complex formation
André, Ingemar LU
; Kesvatera, Tönu
LU
; Jönsson, Bo
LU
; Akerfeldt, KS
and Linse, Sara
LU
(2004)
In Biophysical Journal
87(3).
p.1929-1938
- Abstract
- The complex between calmodulin and the calmodulin-binding portion of smMLCKp has been studied. Electrostatic interactions have been anticipated to be important in this system where a strongly negative protein binds a peptide with high positive charge. Electrostatic interactions were probed by varying the pH in the range from 4 to 11 and by charge deletions in CaM and smMLCKp. The change in net charge of CaM from similar to-5 at pH 4.5 to -15 at pH 7.5 leaves the binding constant virtually unchanged. The affinity was also unaffected by mutations in CaM and charge substitutions in the peptide. The insensitivity of the binding constant to pH may seem surprising, but it is a consequence of the high charge on both protein and peptide. At low pH... (More)
- The complex between calmodulin and the calmodulin-binding portion of smMLCKp has been studied. Electrostatic interactions have been anticipated to be important in this system where a strongly negative protein binds a peptide with high positive charge. Electrostatic interactions were probed by varying the pH in the range from 4 to 11 and by charge deletions in CaM and smMLCKp. The change in net charge of CaM from similar to-5 at pH 4.5 to -15 at pH 7.5 leaves the binding constant virtually unchanged. The affinity was also unaffected by mutations in CaM and charge substitutions in the peptide. The insensitivity of the binding constant to pH may seem surprising, but it is a consequence of the high charge on both protein and peptide. At low pH it is further attenuated by a charge regulation mechanism. That is, the protein releases a number of protons when binding the positively charged peptide. We speculate that the role of electrostatic interactions is to discriminate against unbound proteins rather than to increase the affinity for any particular target protein. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/139609
- author
- André, Ingemar
LU
; Kesvatera, Tönu
LU
; Jönsson, Bo
LU
; Akerfeldt, KS
and Linse, Sara
LU
- organization
- publishing date
- 2004
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biophysical Journal
- volume
- 87
- issue
- 3
- pages
- 1929 - 1938
- publisher
- Cell Press
- external identifiers
-
- wos:000223668500048
- pmid:15345569
- scopus:4444270810
- ISSN
- 1542-0086
- DOI
- 10.1529/biophysj.104.040998
- 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), Biophysical Chemistry (LTH) (011001011)
- id
- 2ff9cf3a-b2ab-4bcd-b8dd-b051037d1fc5 (old id 139609)
- date added to LUP
- 2016-04-01 12:06:18
- date last changed
- 2023-01-03 03:57:00
@article{2ff9cf3a-b2ab-4bcd-b8dd-b051037d1fc5,
abstract = {{The complex between calmodulin and the calmodulin-binding portion of smMLCKp has been studied. Electrostatic interactions have been anticipated to be important in this system where a strongly negative protein binds a peptide with high positive charge. Electrostatic interactions were probed by varying the pH in the range from 4 to 11 and by charge deletions in CaM and smMLCKp. The change in net charge of CaM from similar to-5 at pH 4.5 to -15 at pH 7.5 leaves the binding constant virtually unchanged. The affinity was also unaffected by mutations in CaM and charge substitutions in the peptide. The insensitivity of the binding constant to pH may seem surprising, but it is a consequence of the high charge on both protein and peptide. At low pH it is further attenuated by a charge regulation mechanism. That is, the protein releases a number of protons when binding the positively charged peptide. We speculate that the role of electrostatic interactions is to discriminate against unbound proteins rather than to increase the affinity for any particular target protein.}},
author = {{André, Ingemar and Kesvatera, Tönu and Jönsson, Bo and Akerfeldt, KS and Linse, Sara}},
issn = {{1542-0086}},
language = {{eng}},
number = {{3}},
pages = {{1929--1938}},
publisher = {{Cell Press}},
series = {{Biophysical Journal}},
title = {{The role of electrostatic interactions in calmodulin-peptide complex formation}},
url = {{https://lup.lub.lu.se/search/files/2783112/624739.pdf}},
doi = {{10.1529/biophysj.104.040998}},
volume = {{87}},
year = {{2004}},
}