Vibrational spectra of proteins and topologically disordered solids display a common anomaly at low frequencies, known as Boson peak. We show that such feature in globular proteins can be deciphered in terms of an energy landscape picture, as it is for glassy systems. Exploiting the tools of Euclidean random matrix theory, we clarify the physical origin of such anomaly in terms of a mechanical instability of the system. As a natural explanation, we argue that such instability is relevant for proteins in order for their molecular functions to be optimally rooted in their structures. 87.15.He;63.50.+x,64.70.Pf Proteins are characterized by mechanically stable, unique native structures that bear a precise relation with their biological functions. Yet, in most cases, specific functionality is accompanied by large-amplitude dynamical conformational changes that require high flexibility [1]. Protein structures are complex, hierarchical ones, characterized by short-range order and overall spatial correlations that bear strong similarities with those of glassy materials [2]. In actual fact, proteins and glasses share many physical properties, such as peculiar relaxation processes [3] and the occurrence of a dynamical transition as revealed by the temperature dependence of the atomic mean square displacements (MSD) [1,4,5].Interestingly, there exists a remarkable similarity of the Raman and neutron-scattering spectra of proteins with those of glasses and super-cooled liquids [4], i.e. a peak that develops at low temperatures in the low-frequency regions. Such anomaly, known as Boson peak (BP), also shows up in the experimentally determined density of states when divided by the Debye law, i.e. g(ω)/ω 2 [6]. Several models have been proposed for the explanation of the BP in proteins, among which the phonon-fracton model [7], and the log-normal distribution model [8].The BP is, on the other hand, a universal feature of many glassy systems [9]. In this context, several possible explanations have been proposed, from the two-level system scenario [10] to localized modes arising from a strong scattering of the phonons by the disorder [11], from "glassy" van Hove singularities [12] to a mechanical instability [13]. Recently, the possibility that a BP may be a general feature of weakly connected systems has also been investigated [14,15].In a different analytical framework [16], the excess of low-energy modes with respect to the Debye behaviour is viewed as a symptomatic effect of the topological phase transition which is conjectured to happen in glasses at low temperatures [13]. Recently, a quantitative description of the BP phenomenology has been given whithin the formalism of the Euclidean Random Matrix (ERM) theory [16], whose predictions have been confirmed by numerical simulations on realistic glass-forming systems, emphasizing its universal character [17].In this Letter, we show that the emergence of a BP in globular proteins is the signature of a structural instability of the saddle-phonon kind akin to that predicted w...