  We analyze large systems of interacting proteins, using techniques from the
non-equilibrium statistical mechanics of disordered many-particle systems.
Apart from protein production and removal, the most relevant microscopic
processes in the proteome are complex formation and dissociation, and the
microscopic degrees of freedom are the evolving concentrations of unbound
proteins (in multiple post-translational states) and of protein complexes. Here
we only include dimer-complexes, for mathematical simplicity, and we draw the
network that describes which proteins are reaction partners from an ensemble of
random graphs with an arbitrary degree distribution. We show how generating
functional analysis methods can be used successfully to derive closed equations
for dynamical order parameters, representing an exact macroscopic description
of the complex formation and dissociation dynamics in the infinite system
limit. We end this paper with a discussion of the possible routes towards
solving the nontrivial order parameter equations, either exactly (in specific
limits) or approximately.
