HYDRATION QUANTIZATION OF RECEPTOR BINDING SITES
J. C. Collins, PhD
Dedicated to Professors Carl Djerassi and
William Johnson of
Visit www.LinearWater.com for background and additional references
This web site is an extension of the one cited above in which the concepts of Transient Linear Hydration on surfaces and Proton Quantization in liquid water are used to interpret the motions and interactions of molecules and ions in living cells. In this web site, the concepts will be applied to regulator binding sites in receptor proteins to interpret their occupied and open hydrated forms.
Crystallographic and NMR studies have revealed the structures of a number of regulator binding sites in receptor proteins and have provided information on how those sites control cell function. However, structural determinations are extremely difficult and often must be performed on genetically-modified proteins. When not occupied by regulator molecules, the binding sites are occupied by water molecules which stabilize them in several different conformations. But water molecules are extremely dynamic - thus, identifying positions within the sites has been extremely difficult.
However, forty years ago, in an extensive molecular model-building program, the dimensions of regulator molecules, like neurotransmitters, hormones and drugs, were found to mimic those of linear, hydrogen-bonded segments of water molecules. Since water molecules adopt ordered conformations adjacent to surfaces, a proposal was presented in 1993 that transient linear elements of water molecules occupy binding sites in their open states. Coupled with recent evidence that water molecules move in quantized steps to form hydrogen-bonded units and that the protons of water molecules in the liquid state exhibit the quantum mechanical property of linear wave entanglement, probability hydration models have been developed for the binding sites of five receptor proteins where structures have been determined and for regulator molecules such as the enkephalins, morphine, curare and strychnine where the details of binding have not been established.
Although the models proposed are hypothetical and must be evaluated experimentally, they satisfy present data. Of course, as pointed out in the web site above, the concept that water and protons may be involved in providing spatial order in cells is not new, it was proposed by Schrodinger in 1944 and, again in 1972, by Szent Gyorgi.1,2 For those interested in the potential role of linearizing water in the folding of natural polypeptides to produce proteins, a section has been added at the end. For a story of the role linearizing water may have played in the formation of natural molecules, check out www.MolecularCreation.com.
