ULTIMATE COMPUTING - Quantum Consciousness Studies

136 Protein Conformational Dynamics
induced excited states (“excitons”) were coupled by infrared dipoles in protein
biostructures to provide a communicative medium. McClare concluded:
there is yet another level of organization in biological systems: a
tuned resonance between energy levels in different molecules that
enables bioenergetic machines to operate rapidly and yet efficiently.
This concept was supported by several allies including Wei (1974) who
suggested dipole coupling among membrane proteins to explain nerve functions.
McClare’s general model of resonant dipole coupling was greeted by skepticism,
however. Highly respected biochemist Gregorio Weber (1974) raised two
objections. He noted that at least some of the emitted energy following molecular
excitation is emitted in 10 -12 seconds, too short to be utilized by biomolecules. The
second objection referred to the transfer of quantum vibrational energy through
the surrounding medium. The process of dipole-dipole coupling involves a
similarity of the energies emitted and received, and requires that the interacting
oscillators be surrounded by a medium transparent to the wavelength of the
transferred energy quantum. Water surrounds every biomolecule and provides a
medium which appeared to be opaque to the infrared energy McClare described.
Weber implied any emitted energy would be dissipated as heat to the water
environment. McClare countered, unconvincingly, that systems could have
evolved to be able to slow down the relaxation and energy emission, and that such
systems may be somehow separated from the aqueous phase. A consensus was
that energy needed to be stored for a nanosecond or longer to be useful.
The mode of energy and information transfer was described in other
comparable ways by different scientists. Several considered propagating packages
of conformational or acoustic energy: “phonons.” A phonon can be defined as a
propagated lattice vibration, an intranuclear vibration of a carbon-nitrogen bond
that propagates in a protein lattice. The transmission of phonons occurs at the
speed of sound, so they are not resonance transfer phenomena but a propagated
vibration in a periodic lattice. In 1967 Straub postulated that protein lattices
contain phonons which must be isolated from their aqueous environment. At the
New York Academy meeting in 1973 he suggested that hydrophobic interactions
like Van der Waals forces could contain phonons in the lattice and shield them
from the aqueous bath. The concept of “conformon,” a quantum of protein
conformational energy coupled to discrete protein states was independently
described by Green (1970) and Ji (1974) in America, and Volkenstein (1972) in
the Soviet Union. Later, A. S. Davydov of the Soviet Union proposed that
mechanical conformational movements in proteins were nonlinearly coupled to
electronic bond distortion or charge movement, resulting in propagating waves
called “solitons.” These models all faced a common problem of shielding from
the aqueous environment. One possible resolution of this problem is that the water
surrounding proteins may be “ordered” and resonantly coupled rather than
thermally dissipating protein excitation energy. Another is that hydrophobic
interactions exclude water from areas where important bioenergetic interactions
occur.
6.5 Living Water and Hydrophobic Interactions
Biomolecules have evolved and flourished in aqueous environments, and
basic interactions among biomolecules and their pervasive hosts, water molecules,
are extremely important. The properties of intracellular water are controversial.
Many authors believe that more than 90 percent of intracellular water is in the
“bulk” phase-water as it exists in the oceans (Cooke and Kuntz, 1974; Schwan
and Foster, 1977; Fung and McGaughy, 1979). This traditional view is challenged