Nature is able to convert chemical energy into mechanical work under modest conditions, i.e., physiological pH and ambient temperature and pressure. One of the most interesting systems is muscle modeled as the "sliding filament" system. The sliding filament system is a combination of a thin actin filament and a thick myosin filament that slide over one another by breaking the "energy-rich" pyrophosphate bond of ATP. The energy from ATP hydrolysis is used for mechanical motion and the energy lost during this process is used to heat our body. In biology, the sliding filament system is taken as a fairly effective model. For engineering systems, the energy lost to heat needs to be reduced to build an efficient energy converter. In our research, we use a phosphate charged protein, casein, and react it with divinyl sulfone (DVS) through a Michael addition reaction to produce a cross-linked gel. The protein gel could be ephosphorylated at standard conditions using bovine phosphatase (bp) and re-phosporylated using casein kinase. When attached to the protein, the negatively charged phosphate groups cause the gel to expand from repulsion. When removed, the protein contracts. Therefore, work is realized without sliding friction, which is the origin of the large energy loss in muscle. FT-IR spectroscopy allows us to follow the two biochemical reactions. We also show a thermodynamic analysis of the work and offer an estimation of the most basic term.