Synthetic and binding studies on the postulated calcium binding site I of calmodulin.
The synthesis of the dodecapeptide [sequence (20--31)] representing the hypothetical calcium binding site I of calmodulin by classical methods in solution is described. The interaction of this synthetic calmodulin fragment with calcium ions has been investigated by CD in water and in 98% trifluoroethanol solution. Calcium ions have no effect on the dichroic absorption of the dodecapeptide in aqueous solution in the wavelength range 200-250 nm. However, in 98% trifluoroethanol a linear variation of the CD properties has been observed as a function of the Ca2/peptide molar ratio. The CD results indicate the formation of a 1 : 1 calcium-dodecapeptide complex with a very high binding constant.
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism*; D002147:Calmodulin / Q000378:metabolism*; D002942:Circular Dichroism; D007202:Indicators and Reagents; D009842:Oligopeptides / Q000138:chemical synthesis* / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation
D002147:Calmodulin; D007202:Indicators and Reagents; D009842:Oligopeptides; D002118:Calcium