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Evidence of coupling between the motions of water and peptides

AuthorsCombarro-Palacios, Izaskun; Swenson, Jan; Cerveny, Silvina
Issue Date2017
Citation8th International Discussion Meeting on Relaxations in Complex Systems (2017)
AbstractThe number of studies related with hydrated proteins is numerous but despite of this, the role of water is not clear enough. Moreover, the major problem of the dynamical studies on proteins is its low solubility degree. Due to this, to obtain a proper protein solution, a large quantity of water is necessary which crystallizes on cooling, masking the dielectric signal of the protein itself and hindering the dynamic study. Therefore, most studies are carried out on hydrated powders instead of well-diluted solutions which represent more realistic cases. Here, we avoid the problem of crystallization by reducing the size of the biomolecules. We have studied oligomers of the amino acid n-lysine oligomers, fully dissolved in water. The dielectric relaxation data show that the glass transition-related dynamics of the oligomers is determined by the water dynamics, in a way similar to that previously observed for solvated proteins: above the glass transition temperature, the protein motions follow the same temperature dependence as the surrounding water molecules. According to this, a coupling between the solute and the solvent dynamics can be defined, describing the motion of oligomers as being “slaved” to that of the solvents surrounding the solute molecules. This implies that the crucial role of water for protein dynamics can be extended to other types of macromolecular systems, where water is also able to determine their conformational fluctuations.
DescriptionResumen del póster presentado al 8th International Discussion Meeting on Relaxations in Complex Systems: "New results, Directions and Opportunities", celebrado en Wisla (Polonia) del 23 al 28 de julio de 2017.
Appears in Collections:(CFM) Comunicaciones congresos
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