| Abstract: | The structure of bovine brain calmodulin was probed by using laser Raman spectroscopy to elucidate cation-induced conformational changes in the protein. Local changes, most likely reflecting metal binding but not rearrangement of the peptide backbone, were observed in the presence of calcium or magnesium. A conformational change involving the peptide backbone and secondary structure content of calmodulin was observed only in the presence of calcium. The calcium-induced conformational change in the peptide backbone involves increased alpha helix and beta sheet. This was the only major calcium-specific change observed in the Raman spectrum, which suggests that the flexibility of the backbone conformation may play a critical role in the physiological activity of calmodulin. |
