The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.
Calcium binding to calmodulin and its globular domains
Open accessAbstract
The macroscopic Ca(2+)-binding constants of bovine calmodulin have been determined from titrations with Ca2+ in the presence of the chromophoric chelator 5,5'-Br2BAPTA in 0, 10, 25, 50, 100, and 150 mM KCl. Identical experiments have also been performed for tryptic fragments comprising the N-terminal and C-terminal domains of calmodulin. These measurements indicate that the separated globular domains retain the Ca2+ binding properties that they have in the intact molecule. The Ca2+ affinity is 6-fold higher for the C-terminal domain than for the N-terminal domain. The salt effect on the free energy of binding two Ca2+ ions is 20 and 21 kJ. mol-1 for the N- and C-terminal domain, respectively, comparing 0 and 150 mM KCl. Positive cooperativity of Ca2+ binding is observed within each globular domain at all ionic strengths. No interaction is observed between the globular domains. In the N-terminal domain, the cooperativity amounts to 3 kJ.mol-1 at low ionic strength and greater than or equal to 10 kJ.mol-1 at 0.15 M KCl. For the C-terminal domain, the corresponding figures are 9 +/- 2 kJ.mol-1 and greater than or equal to 10 kJ.mol-1. Two-dimensional 1H NMR studies of the fragments show that potassium binding does not alter the protein conformation.
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Cites
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Three-dimensional structure of calmodulin
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Metadata
- Authors
- Linse, S., Helmersson, A., & Forsén, S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1991-05
- Volume
- 266
- Issue
- 13
- Pages
- 8050-8054
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1565248232
- Cited by
- 485
- References
- 16
- FWCI
- 3.55
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Linse, S., Helmersson, A., & Forsén, S. (1991). Calcium binding to calmodulin and its globular domains. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)92938-8
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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