Measurement of Ca2+-binding constants of proteins and presentation of the CaLigator software.
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/108699
- author
- André, Ingemar LU and Linse, Sara LU
- organization
- publishing date
- 2002
- 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
- 2016-04-01 11:41:56
- date last changed
- 2022-01-26 08:56:02
@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}}, doi = {{10.1006/abio.2002.5661}}, volume = {{305}}, year = {{2002}}, }