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With the help of force spectroscopy, several analytical theories aim at estimating the rate coefficient of folding for various proteins. Nevertheless, a chief bottleneck lies in the fact that there is still no perfect consensus on how does a force generally perturb the crystal-coil transition. Consequently, the goal of our work is in clarifying the generic behavior of most proteins in force spectroscopy; in other words, what general signature does an arbitrary protein exhibit for its rate coefficient as a function of the applied force? By employing a biomimetic polymer in molecular simulations, we focus on evaluating its respective activation energy for unfolding, while pulling on various pairs of its monomers. Above all, we find that in the vicinity of the force-free scenario, this activation energy possesses a negative slope and a negative curvature as a function of the applied force. Our work is in line with the most recent theories for unfolding, which suggest that such a signature is expected for most proteins, and thus, we further reiterate that many of the classical formulae, that estimate the rate coefficient of the crystal-coil transition, are inadequate. Besides, we also present here an analytical expression which experimentalists can use for approximating the activation energy for unfolding; importantly, it is based on measurements for the mean and variance of the distance between the beads which are being pulled. In summary, our work presents an interesting view for protein folding in force spectroscopy.