Due to the large number of energy evaluations required, GAs for peptide folding are commonly used in conjunction with classical force fields or expedient semiempirical methods, at the price of loosing accuracy so that identified stable structures might correspond to false LM introduced by the energy function and relative energies between different conformers be far off experimental observations. As a potential remedy, GA optimizations were recently combined with DFT local relaxations. However, this approach was rather limited to short GA instances of dipeptides and molecules up to ∼40 atoms so that applications of this fully DFT-based approach to larger systems are currently compromised even when resorting to massively parallel computational resources.