Study of the impact of the crystallization of the surrounding water on the mini protein TRP-cage

C. GASTÓN FERRARA; DIDONE PEDRO; ATTARANTATO VALENTIN

ROSARIO

Congreso; REUNION ANUAL de la SOCIEDAD ARGENTINA de BIOFISICA; 2022

SAB

We present the initial study of the impact of the crystallization of water over mini protein TRP-cage structure and the kinetic crystallization of water. The objective of this work is to advance the understanding of the role played by the different domains of a protein in its interaction with water crystals and its influence on denaturation. For it, we used TRP-cage which is a protein stable over a wide temperature range and wich is very helpful if we want to observe the different changes in its structure or functionality. In order to study this problem, we perform a series of simulations using the Molecular Dynamics (DM) technique. For these systems, the structure TRP-cage was obtained from the 1L2y model, obtained by NMR, and using the TIP4P/2005 water model as an explicit solvent. As crystallization seed we used a flat wall made up of TIP4P/2005 water molecules.To analyze the role played by the solvent in the possible transition from a folded to an unfolded state in TRP-cage, at temperatures below room temperature, we analyzed parameters such as the solvent-exposed surface (total, hydrophobic and hydrophilic), gyration radii, rmsd, rmsf and hydrogen bond distribution, in order to observe structural changes. All these parameters were analyzed for the protein in bulk condition and when crystallized water is found in its environment.Our initial results indicate that the liquid-solid transition of water molecules influences the native protein structure due to changes in intramolecular and intermolecular interactions at low temperatures, changes in its hydration cause structural changes in the proteins at low temperatures.