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Conformational and binding studies on peptides related to domains I and III of calmodulin

✍ Scribed by Maria Teresa Foffani; Roberto Battistutta; Andrea Calderan; Paolo Ruzza; Gianfranco Borin; Evaristo Peggion

Publisher
Wiley (John Wiley & Sons)
Year
1991
Tongue
English
Weight
732 KB
Volume
31
Category
Article
ISSN
0006-3525

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✦ Synopsis

The conformational and ion-binding properties of two peptide fragments of 25 amino acid residues corresponding to the helix-loop sequences of domains I and 111 of calmodulin ( CaM) were investigated by CD and Tb3+-mediated fluorescence spectroscopy. Both peptides exhibit very similar ion binding properties either in water or trifluoroethanol (TFE) , and do not allow the differentiation of the two domains in the native protein in terms of their binding capacity. An aggregation phenomenon was observed in TFE with increase of the a-helical content. We suggest that the aggregation involves an interaction between the hydrophilic surfaces of amphiphilic a-helices in a way similar to inverse micelle formation.

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