The dependence of the molecular dynamics of calmodulin upon pH and ionic strength.
The mobilities of several fluorescent probes placed at different locations on calmodulin in the absence of Ca2+ have been found to depend upon the charge, ionic strength, and temperature. In general, the time decay of fluorescence anisotropy could be fitted with two rotational correlation times. The shorter of these reflects primarily the motion of the probe itself, while the longer corresponds to the motion of a major portion of the molecule. An increase in ionic strength or a decrease in net charge results in a decrease in the relative amplitude of the shorter correlation time, while an increase in temperature produces an increase in its amplitude. These results are consistent with, and suggest, that an increase in probe mobility accompanies an expansion of the calmodulin molecule under conditions of high electrostatic stress.
D000818:Animals; D001665:Binding Sites; D002135:Calcium-Binding Proteins; D002147:Calmodulin; D002417:Cattle; D002942:Circular Dichroism; D004563:Electrochemistry; D005454:Fluorescence Polarization; D005456:Fluorescent Dyes; D006863:Hydrogen-Ion Concentration; D008297:Male; D009994:Osmolar Concentration; D011487:Protein Conformation; D013737:Testis / Q000378:metabolism; D014783:Viscosity
D002135:Calcium-Binding Proteins; D002147:Calmodulin; D005456:Fluorescent Dyes