In this paper we show that ensembles of well-structured and unstructured proteins can be distinguished by borrowing concepts from non-equilibrium statistical mechanics. For this purpose, we represent proteins by two different polymer models and interpret the resulting polymer configurations as random walks of a diffusing particle in space. The first model is the trace of the Cα-atoms along the protein main chain and the second their projections onto the protein axis. The resulting trajectories are subsequently analyzed using the theory of the Generalized Langevin Equation. Velocities are replaced by displacements relating consecutive points on the discrete protein axes and equilibrium ensemble averages by averages over appropriate protein structure ensembles. The resulting displacement autocorrelation functions resemble those of velocity autocorrelation functions of simple liquids and display a minimum, which can be related to the lengths of secondary structure elements. This minimum is clearly more pronounced for well-structured proteins than for unstruc-tured ones and the corresponding memory function displays a slower decay, indicating a stronger "folding memory".