Abstract
Two special dynamical transitions of universal character have been recently observed in macromolecules at K and 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 (), phonon-phonon interactions with phonons of water dimer (), and water rotational barriers surpassing ().
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