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Studies on the interaction of the dye, Stains-all, with individual calcium-binding domains of calmodulinPublished in
1993
Volume: 326
Issue: 1-3
Pages: 59 - 64
We show that the calcium-mimic dye, Stains-all, is a convenient probe to study the structural features of the individual calcium-binding sites of calmodulin (CaM) and related calcium-binding proteins (CaBP). These peptides bind the dye in their calcium-binding sites, and induce a circular dichroism (CD) band in the bound dye in the 620 nm (J band) region, which is abolished upon the addition of calcium. Replacement of Asp by Asn in the +x position of the weaker calcium-binding site (site I of CaM) abolishes the dye binding, while the same change in the higher affinity site IV attenuates the binding of the dye and does not abolish it. Replacement of Tyr in site IV with Trp does not distort the geometry, although it increases the dye binding affinity. © 1993.
Topics: Binding site (54)%54% related to the paper, Calmodulin (54)%54% related to the paper, Circular dichroism (50)%50% related to the paper and Binding protein (50)%50% related to the paper
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| Journal | FEBS Letters |
|---|---|
| Open Access | No |
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