Two special dynamical transitions of universal character have been recently observed in macromolecules at TD ∼ 180−220 K and T * ∼ 100 K. Despite their relevance, a complete understanding of the nature of these transitions and their consequences for the bio-activity of the macromolecule is still lacking. Our results and analysis concerning the temperature dependence of structural, vibrational and thermodynamical properties of the orthorhombic polymorph of the amino acid L-cysteine (at a hydration level of 3.5%) indicated that the two referred temperatures define the triggering of very simple and specific events that govern all the biochemical interactions of the biomolecule: activation of rigid rotors (T < T * ), phonon-phonon interactions with phonons of water dimer (T * < T < TD), and water rotational barriers surpassing (T > TD).