We explore the results of our work on four well-studied globular proteins: bovine β-lactoglobulin (PDB:3NPO), hen egg-white lysozyme (PDB:3WUN), hisactophilin (PDB:1HCD), and calmodulin (PDB:3CLN). These four proteins were chosen as charge regulation effects in them have been studied previously both in theory and simulation ] and as their shape can be approximated reasonably well by a sphere. In extracting their charge distributions (see the example in Fig. ), we follow previously established methods ; details of the procedure are given in the SI. Using the four proteins as examples, we analyze their average charge and the corresponding charge fluctuations, their average dipole moment and the dipole moment fluctuations, their polarizability and the associated dielectric constant of the protein, and the strength of the generalized KS charge fluctuation interactions. In what follows, the charges q i in the presence of CR are calculated from Eq. ( ) and charges q (0) i in the absence of CR are obtained from Eq. (S3) in the SI.