RESUMO
The damage produced by UV-C radiation (100-280nm) in organisms and cells is a well known fact. The main reactions of proteins to UV-C radiation consist in the alteration of their secondary structures, exposure of hydrophobic residues, unfolding and aggregation. Furthermore, it has been found that electromagnetic radiation of lower energy (visible light, where wavelengths are between 400 and 750nm) also induces different disturbances in biomolecules. For instance, it has been observed that blue visible light from emitting diodes (LEDs) produces severe damage in murine cone photoreceptor-derived cells, and it can be even more harmful for some organisms than UV radiation. Recently, it has been found that the exposure of proteins to green and red light produces conformational changes, considerably increasing their cohesion enthalpies. This is presumably due to the strengthening of the hydrogen bonds and the formation of new ones. Therefore, it seems that visible light acts contrary to what it is observed for UV-C: instead of unfolding the proteins it folds them further, halting the damage produced by UV-C. This can be understood if we consider the modification of the folding energy-landscape; visible light induces the descent of the proteins into deeper states impeding the unfolding produced by UV-C.