Aquaphotomics: Dynamic Spectroscopy of Aqueous and Biological Systems Describes Peculiarities of Water

ISSn: 0967-0335 © IM publications llp 2009 doi: 10.1255/jnirs.869 all rights reserved Water is the most substantial and widely distributed component of biological systems. It is a complex subject which has received considerable attention over the years. Groups from different scientific areas have been working on its properties, structure, functions etc., yet static analysis on a narrow set of water characteristics has only provided a limited picture of this unique substance. Several methods have been applied to study the physical chemistry of water itself: X-ray spectrometry,1–3 infrared (Ir) spectrum analysis,4,5 raman scattering spectroscopy,6 nuclear magnetic resonance (nMr) spectroscopy,7 dielectric relaxation spectroscopy (drS),8,9 tHz spectroscopy,10 neutron diffraction11 etc. each technique provides us with valuable information on a different aspect of a water system. on the other hand, water is not simply a physical subject. It is a basic constituent of all life structures. In order to understand water from a system point of view, new tools are needed for real time monitoring and non-invasive dynamic analysis of biological and aqueous systems. Human body cells contain up to 90% water, but biological sciences are very much focused on pinpointing single biomolecules related to natural phenomena or disease. the possibility that these phenomena rely on the simultaneous dynamic contribution of various components of the living system, especially of water as a medium, is not fully considered. the structure of biomolecules (i.e. proteins, nucleotides) is highly related to their functions.12 folding and stabilisation of tertiary and quaternary structures is largely due to the creation of hydrogen bonds with the surrounding water molecules. for example, protein tertiary structure formation, the protein function defining structure, is largely a process of exposing hydrophilic areas and burying hydrophobic residues. Hence, protein functional structure formation is a result of interactions with the surrounding water. Water structure still remains unknown, but a spectroscopic point of view agrees that it could be described as a matrix, i.e. molecular network13 of water molecular conformations with different hydrogen-bond populations and special distribution to accommodate and facilitate various functions, including biological ones. as the strength of the hydrogen bond13–15 and its location defines its functionality, it could be described as a multi-functional “body” simultaneously having many “faces”, i.e. many structures.