A simple method has been developed to predict the calmodulin-binding domains of peptides and the affinities of the peptides for calmodulin based on a model for the calmodulin-binding domains of peptides proposed in a previous paper and the literature data of calmodulin-binding peptides. The effects of hydrophobitities, α-helix-forming tendencies, and basicities of peptides on their affinities for calmodulin were studied. Model peptides were designed to examine the calmodulin-binding domain model and the prediction method. The determined dissociation constants of the complexes formed from the model peptides and calmodulin are in good agreement with the predicted results.
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机译:On-line concentration of peptides and proteins with the hyphenation of polymer monolithic immobilized metal affinity chromatography and capillary electrophoresis