Hydrogen bonds are essential to life as we know it, and the formation of hydrogen bond networks is a key driver of structure in biochemistry, ubiquitous in critical cell processes such as nucleotide base pairing and protein folding. However, the coarse-graining procedure in Martini 3 places hydrogens together with heavy atoms into larger Lennard-Jones (LJ) particles and effectively averages out the energy contribution of directional hydrogen bonding. In this work, we investigate whether the secondary and tertiary structure instability in Martini 3 proteins could originate from missing hydrogen bond energy. We introduce an algorithm called OLIVES which identifies native contacts with hydrogen bond capabilities in coarse-grained structures, as an approximation for the atomistic hydrogen bond network, and uses it to implement a novel Gō-like model for Martini 3 proteins. By using realistic hydrogen bond energies obtained from literature ab initio calculations, we show that Martini 3 proteins can be stabilized by the introduction of LJ bonds between hydrogen bonding beads in native contacts.