The role of water in protein's behavior: The two dynamical crossovers studied by NMR and FTIR techniques

The role the solvent plays in determining the biological activity of proteins is of primary importance. Water is the solvent of life and proteins need at least a water monolayer covering their surface in order to become biologically active. We study how the properties of water and the effect of its...

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Veröffentlicht in:	Computational and structural biotechnology journal 2015-01, Vol.13 (C), p.33-37
Hauptverfasser:	Mallamace, Francesco, Corsaro, Carmelo, Mallamace, Domenico, Vasi, Sebastiano, Vasi, Cirino, Dugo, Giacomo
Format:	Artikel
Sprache:	eng
Schlagworte:	Amide bending mode bioactive properties denaturation enzyme activity Fourier transform infrared spectroscopy HR-MAS Hydration water hydrogen bonding hydrophilicity lysozyme Lysozyme unfolding nuclear magnetic resonance spectroscopy Protein dynamic transition proteins solvents temperature water
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Beschreibung
Zusammenfassung:	The role the solvent plays in determining the biological activity of proteins is of primary importance. Water is the solvent of life and proteins need at least a water monolayer covering their surface in order to become biologically active. We study how the properties of water and the effect of its coupling with the hydrophilic moieties of proteins govern the regime of protein activity. In particular we follow, by means of Fourier Transform Infrared spectroscopy, the thermal evolution of the amide vibrational modes of hydrated lysozyme in the temperature interval 180 K
ISSN:	2001-0370 2001-0370
DOI:	10.1016/j.csbj.2014.11.007