Mutational effects on the cooperativity of calcium binding in calmodulin
β Scribed by Waltersson, Yvonne; Linse, Sara; Brodin, Peter; Grundstroem, Thomas
- Book ID
- 127012039
- Publisher
- American Chemical Society
- Year
- 1993
- Tongue
- English
- Weight
- 696 KB
- Volume
- 32
- Category
- Article
- ISSN
- 0006-2960
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## Abstract Calmodulin is a member of the βEFβhandβ family of Ca^2+^βbinding proteins. It consists of two homologous globular domains, each containing two helixβloopβhelix Ca^2+^βbinding sites. To examine the contribution of individual Ca^2+^βbinding sites to the Ca^2+^βbinding properties of CaM, a
By the use of calcium and sodium specific electrodes, the study of the ionic interactions with well-characterized pectins has shown a greater affinity of pectins towards calcium ions when the degree of methylation of the samples and the ionic strength of the systems decreased. The affinity of pectic