Partial specific volume and adiabatic compressibility of G-actin depend on the bound nucleotide.

We determined the partial specific volume and partial specific adiabatic compressibility of either ATP- or ADP-bound monomeric actin in the presence of Ca(2+) by measuring the density of and sound velocity in a monomeric actin solution at 18 degrees C. The partial specific volume of ATP-bound monomeric actin, equal to 0.744 cm(3)/g, which is exceptionally high among globular proteins, was reduced to 0.727 cm(3)/g when the tightly bound ATP was replaced with ADP. Associated with this, the adiabatic compressibility of ATP-bound monomeric actin, equal to 8.8 x 10(-12) cm(2)/dyne, decreased to 5.8 x 10(-12) cm(2)/dyne, which is a common value for globular proteins. These results suggested that an extraordinarily soft global conformation of ATP-bound monomeric actin is packed into a compact mass associated with the hydrolysis of bound ATP. When monomeric actin was limitedly proteolyzed at subdomain 2 with subtilisin, the nucleotide-dependent flexibility of the global conformation of monomeric actin was lost.