Interaction of water with surface-exposed amino acids crosslinked to porous silicon
Recently, we have elaborated a thermodynamic theory that coherently interprets the diverse effects of Hofmeister ions on proteins, based on the protein-water interfacial tension. The theory predicts changes in protein conformational fluctuations in the presence of Hofmeister salts. We confirmed this prediction via various methods, including EINS (IN13) [Szalontai et al. 2013]. We demonstrated that Hofmeister salts, via setting the hydrophobic/hydrophilic properties of the protein-water interface, control conformational fluctuations of the typical membrane transport protein bacteriorhodopsin. According to our hypothesis the interfacial water structure has a determining role in defining protein structure and conformational dynamics. Here we propose to address this point from another aspect. Surface-exposed amino acids are also expected to control the structure of the adjacent water layer. Hence, we propose to perform EINS experiments monitoring the water structure and dynamics in the vicinity of target protein or peptide molecules. Dynamical changes of the interfacial water layer will help to classify water-exposed surfaces of proteins of different conformational character.
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NAGY Gergely; DER Andras; FABIAN Laszlo; PETERS Judith and SEYDEL Tilo. (2016). Interaction of water with surface-exposed amino acids crosslinked to porous silicon. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-731
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