  Proteins are aminoacid chains that diffusively fold or unfold depending on
the thermal and chemical environmental conditions. While sophisticated models
account for detailed aspects of real proteins, finding traits that unify
protein dynamics to general open chains relaxation is still challenging. The
principle of minimal frustration represents a key step towards this goal,
revealing a fundamental link between proteins and spin glasses. Here, we search
for the emergence of protein-like relaxation in open spin chains by going
beyond the validity domain of the minimal frustration principle as to focus on
the role of system-environment interactions rather than on frustration in the
system's Hamiltonian. We find that strong asymmetries between the couplings of
each spin to its immediate surroundings imply close similarities to protein
folding and unfolding dynamics. Namely, an asymmetric bath can (i) block the
system from finding its minimum energy state, even in the complete absence of
energetic frustration in the system's Hamiltonian, and (ii) excite the system
resembling the well-known distinction between thermal and chemical
denaturations.
