Conformational and binding studies on peptides related to domains I and III of calmodulin.
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 alpha-helical content. We suggest that the aggregation involves an interaction between the hydrophilic surfaces of amphiphilic alpha-helices in a way similar to inverse micelle formation.
Biopolymer Research Center, University of Padua, Italy.
M T
MT
Foffani
R
R
Battistutta
A
A
Calderan
P
P
Ruzza
G
G
Borin
E
E
Peggion
D000595:Amino Acid Sequence; D000818:Animals; D002147:Calmodulin / Q000737:chemistry*; D002417:Cattle; D002942:Circular Dichroism; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D012996:Solutions; D013050:Spectrometry, Fluorescence; D014270:Trifluoroethanol; D014867:Water
D002147:Calmodulin; D010455:Peptides; D012996:Solutions; D014867:Water; D014270:Trifluoroethanol