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Conformational and binding studies on peptides related to domains I and III of calmodulin
Author(s) -
Foffani Maria Teresa,
Battistutta Roberto,
Calderan Andrea,
Ruzza Paolo,
Borin Gianfranco,
Peggion Evaristo
Publication year - 1991
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360310612
Subject(s) - chemistry , calmodulin , amphiphile , biophysics , micelle , peptide , helix (gastropod) , conformational change , circular dichroism , amino acid residue , amino acid , crystallography , peptide sequence , stereochemistry , biochemistry , calcium , organic chemistry , aqueous solution , polymer , ecology , snail , copolymer , biology , gene
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 III of calmodulin (CaM) were investigated by CD and Tb 3+ ‐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 α‐helical content. We suggest that the aggregation involves an interaction between the hydrophilic surfaces of amphiphilic α‐helices in a way similar to inverse micelle formation.