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. 1985 Aug;82(15):4954–4958. doi: 10.1073/pnas.82.15.4954

A predicted structure of calmodulin suggests an electrostatic basis for its function.

K T O'Neil, W F DeGrado
PMCID: PMC390476  PMID: 3860834

Abstract

By using interactive computer graphics, two models for calmodulin have been constructed based on the structures of two functionally and structurally related proteins, intestinal calcium-binding protein and carp parvalbumin. The two models have been compared and contrasted to the parent proteins with respect to proportion of solvent-exposed hydrophobic residues, solvent-accessible surface area, and side-chain packing. Electrostatic potential surfaces generated for the models suggest a probable binding site for basic amphiphilic alpha-helical peptides located between the last E and F helices in the second domain of calmodulin. Both electrostatic and hydrophobic complementarity can contribute to stabilization of a peptide-protein complex in this region.

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Selected References

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