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ULTIMATE COMPUTING - Quantum Consciousness Studies

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Protein Conformational Dynamics 137<br />

by others who feel that none of the water in living cells is bulk (Troshin, 1966,<br />

Cope 1976, Negendank and Karreman, 1979). A middle position is assumed by<br />

those who feel that about half of “living” water is bulk and the other half<br />

“ordered” (Hinke, 1970; Clegg, 1976; Clegg, 1979; Horowitz and Paine, 1979).<br />

This group emphasizes the importance of “ordered” water to cellular structure and<br />

function.<br />

Many techniques have been used to study this issue, but the results still<br />

require a great deal of interpretation. Nuclear magnetic resonance (NMR), neutron<br />

diffraction, heat capacity measurement, and diffusion studies are all inconclusive.<br />

Water appears to exist in both ordered and aqueous forms within cells. The<br />

critical issue is the relation between intracellular surfaces and water. Surfaces of<br />

all kinds are known to perturb adjacent water, but within cells it is unknown<br />

precisely how far from the surfaces ordering may extend. We know the surface<br />

area of the microtrabecular lattice and other cytoskeleton components is extensive<br />

(billions of square nanometers per cell) and that about one fifth of cell interiors<br />

consist of these components. Biologist James Clegg (1981) has extensively<br />

reviewed these issues. He concludes that intracellular water exists in three phases.<br />

1) “Bound water” is involved in primary hydration, being within one or two<br />

layers from a biomolecular surface. 2) “Vicinal water” is ordered, but not directly<br />

bound to structures except other water molecules. This altered water is thought to<br />

extend 8 to 9 layers of water molecules from surfaces, a distance of about 3<br />

nanometers. Garlid (1976, 1979) has shown that vicinal water has distinct solvent<br />

properties which differ from bulk water. Thus “borders” exist between water<br />

phases which partition solute molecules. 3) “Bulk water” extends beyond 3<br />

nanometers from cytoskeletal surfaces (Figure 6.4).<br />

Drost-Hansen (1973) described cooperative processes and phase transitions<br />

among vicinal water molecules. Clegg points out the potential implications of<br />

vicinal water on the function of enzymes which had previously been considered<br />

“soluble.” Rather than floating freely in an aqueous soup, a host of intracellular<br />

enzymes appear instead to be bound to the MTL surface within the vicinal water<br />

phase. Significant advantages appear evident to such an arrangement: a sequence<br />

of enzymes which perform a sequence of reactions on a substrate would be much<br />

more efficient if bound on a surface in the appropriate order. Requirements for<br />

diffusion of the substrate, the most time consuming step in enzymatic processes,<br />

would be minimal. Clegg presents extensive examples of associations of<br />

cytoplasmic enzymes which appear to be attached to and regulated by, the MTL.<br />

These vicinal water multi-enzyme complexes may indeed be part of a cytoskeletal<br />

information processing system. Clegg conjectures that dynamic conformational<br />

activities within the cytoskeleton/MTL can selectively excite enzymes to their<br />

active states.<br />

The polymerization of cytoskeletal polymers and other biomolecules appears<br />

to flow upstream against the tide of order proceeding to disorder which is decreed<br />

by the second law of thermodynamics. This apparent second law felony is<br />

explained by the activities of the water molecules involved (Gutfreund, 1972).<br />

Even in bulk aqueous solution, water molecules are somewhat ordered, in that<br />

each water molecule can form up to 4 hydrogen bonds with other water<br />

molecules. Motion of the water molecules (unless frozen) and reversible breaking<br />

and reforming of these hydrogen bonds maintain the far miliar liquid nature of<br />

bulk water. Outer surfaces of biomolecules form more stable hydrogen bonding<br />

with water, “ordering” the water surrounding them. This results in a decrease in<br />

entropy (increased order) and increase in free energy: factors which would<br />

strongly inhibit the solubility of biomolecules if not for the effects of hydrophobic<br />

interactions. Hydrophobic groups (for example amino acids whose side groups are

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