Superimposed structures of pairs of RBPs in RNA-complexed structure and their unbound monomeric forms. Figure on the left shows complexed and unbound monomeric pairs of 30S ribosomal protein S16 (Complex PDB ID 1hnw_P in red, unbound PDB ID 1emw_A in blue) and on the right a pair of Zinc finger structures in complex (1un6_B, blue) and unbound forms (2j7j_A, red) have been shown. Dipole and quadrupole moment values for Ribosomal protein S16 remain almost unchanged despite undergoing conformational changes (Table 5), whereas zinc finger pairs show a significant difference in the two variations. However, this protein (zinc finger) is a rare example of very large conformational changes in RBPs and in the compared pairs in Table 4, is the only exception to all other pairs, where complex and unbound structures have similar values of moments. This exception was further analyzed to reveal that the moments in the individual domains remain largely unchanged.