  The emergence of biochemical activities in a protein seem to commence with
the onset of atomic mean-square displacements along the protein lattice. The
ensuing protein dynamical transition has been discussed extensively in the
literature, and often with conflicting conclusions. Here we clarify the
phenomenon by establishing a deep connection between the dynamical transition
and the pseudogap state where high-temperature superconductivity comes to its
end.
  For this we first show how to endow proteins with an order parameter akin the
quasiparticle wave function in superconductors. We then present universality
arguments to claim that the protein dynamical transition takes place in tandem
with a pseudogap transmutation. We confirm that available experimental data
fully supports our proposal.
