The ribosome is a universal molecular machine (comprised of RNA and proteins) which translates the message from the genome into proteins (polymers of amino acids) in biology. Similar to how Flight and Cockpit voice recorders record and preserve an aircraft’s flight history, the ribosome has recorded signatures of its evolution. Tapping this resource is important for understanding the origins of life. The electrostatic properties/net positive charge(s) of ribosomal proteins (RPs) stabilize interactions with the negatively charged ribosomal RNA (rRNA) and influence the assembly and folding of ribosomes. A high percentage of RPs from extremely halophilic archaea are known to be acidic/negatively charged. Recently the net charges (at pH 7.4) of the RPs from a highly conserved cluster of RPs were found to have an inverse relationship with the halophilicity/halotolerance (ability to survive under salt conditions) levels in bacteria and archaea. In non-halophilic bacteria, these RPs are generally basic, contrasting with the acidic proteomes of the extreme halophiles. We explore the use of a new mathematical modeling technique based on interaction graphs to provide a systematic understanding of the structural differences in the Large Subunit (LSU) of the bacterium Escherichia coli and that of the extremely halophilic archaeon Haloarcula marismortui.