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Measurement of Ca2+-binding constants of proteins and presentation of the CaLigator software.

André, Ingemar LU and Linse, Sara LU (2002) In Analytical Biochemistry 305(2). p.195-205
Abstract
The complexity of Ca2+ cell signaling is dependent on a plethoria of Ca2+-binding proteins that respond to signals in different ranges of Ca2+ concentrations. Since the function of these proteins is directly coupled to their Ca2+-binding properties, there is a need for accurately determined equilibrium Ca2+-binding constants. In this work we outline the experimental techniques available to determine Ca2+-binding constants in proteins, derive the models used to describe the binding, and present CaLigator, software for least-square fitting directly to the measured quantity. The use of the software is illustrated for Ca2+-binding data obtained for two deamidated forms of calbindin D(9k), either an isospartate-56 (beta form) or a normal Asp-56... (More)
The complexity of Ca2+ cell signaling is dependent on a plethoria of Ca2+-binding proteins that respond to signals in different ranges of Ca2+ concentrations. Since the function of these proteins is directly coupled to their Ca2+-binding properties, there is a need for accurately determined equilibrium Ca2+-binding constants. In this work we outline the experimental techniques available to determine Ca2+-binding constants in proteins, derive the models used to describe the binding, and present CaLigator, software for least-square fitting directly to the measured quantity. The use of the software is illustrated for Ca2+-binding data obtained for two deamidated forms of calbindin D(9k), either an isospartate-56 (beta form) or a normal Asp-56 (alpha form). Here, the Ca2+-binding properties of the two isoforms have been studied using the chelator method. The alpha form shows similar Ca2+-binding properties to the wild type while the beta form has lost both cooperativety and affinity. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Analytical Biochemistry
volume
305
issue
2
pages
195 - 205
publisher
Elsevier
external identifiers
  • wos:000176363900009
  • pmid:12054448
  • scopus:0037096128
ISSN
1096-0309
DOI
10.1006/abio.2002.5661
language
English
LU publication?
yes
id
755a5dc9-45d2-47cc-ba88-51e80c2ed0c8 (old id 108699)
date added to LUP
2007-06-29 08:36:10
date last changed
2017-03-19 03:24:38
@article{755a5dc9-45d2-47cc-ba88-51e80c2ed0c8,
  abstract     = {The complexity of Ca2+ cell signaling is dependent on a plethoria of Ca2+-binding proteins that respond to signals in different ranges of Ca2+ concentrations. Since the function of these proteins is directly coupled to their Ca2+-binding properties, there is a need for accurately determined equilibrium Ca2+-binding constants. In this work we outline the experimental techniques available to determine Ca2+-binding constants in proteins, derive the models used to describe the binding, and present CaLigator, software for least-square fitting directly to the measured quantity. The use of the software is illustrated for Ca2+-binding data obtained for two deamidated forms of calbindin D(9k), either an isospartate-56 (beta form) or a normal Asp-56 (alpha form). Here, the Ca2+-binding properties of the two isoforms have been studied using the chelator method. The alpha form shows similar Ca2+-binding properties to the wild type while the beta form has lost both cooperativety and affinity.},
  author       = {André, Ingemar and Linse, Sara},
  issn         = {1096-0309},
  language     = {eng},
  number       = {2},
  pages        = {195--205},
  publisher    = {Elsevier},
  series       = {Analytical Biochemistry},
  title        = {Measurement of Ca2+-binding constants of proteins and presentation of the CaLigator software.},
  url          = {http://dx.doi.org/10.1006/abio.2002.5661},
  volume       = {305},
  year         = {2002},
}