We present a theoretical approach for looking into the unfolding pathway of simple modular proteins in length-controlled pulling experiments. The first module that unfolds is predicted in a chain of identical modules, for a certain range of pulling speeds. The possibility of checking the above framework experimentally is discussed, and we show some atomic force microscopy experiments with anykirin repeats leading to inconclusive results. Therefore, we move on to analysing Steered Molecular Dynamics of a very simple construct, specifically a chain composed of two coiled-coils motives. These simulations, in which anisotropic features are revealed, allow us to give an estimate for the range of pulling velocities in which our theoretical approach is valid for such a system.