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The
LifeWave Energy Patch
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Patches - Please Click Here!!
Data supporting the concept that cell components can respond
to external frequencies with metabolic changes
In order for an electromagnetic field to activate a metabolic
process in the body a field induced molecular change must occur.
This section will discuss the
physical, chemical and electrical properties of proteins and how
electrical fields can affect the molecular structures and functions
of proteins. "It is at the atomic level that physical processes,
rather than chemical reactions in the fabric of molecules, appear
to shape the transfer of energy and the flow of signals in living
systems (Adey, 1993a)."
Proteins are sophisticated molecules that play critical structural
and functional roles in the cells. Proteins help provide cell
structure, strength and flexibility. Proteins also have functional
roles as signaling molecules in the processes of cell communication
and as enzymes in the chemical reactions of cells. The functional
properties of proteins in turn are dependent upon their three-dimensional
structure (Grattarola et al., 1998).
Proteins that catalyze chemical reactions are called enzymes
(Holyzclaw et al., 1991). The body's enzymes are natural catalytic
molecules that promote chemical reactions without themselves being
used up. Enzymes are specific for certain chemical substances
because they recognize specific chemical structures both by their
three-dimensional shape as well as by their chemical properties
(Jespersen, 1997).
Proteins embedded in cell membranes that act as signal devices
are called receptors. Receptors respond to chemical signals from
the blood stream to initiate chemical pathways within the cells
and to assist in the transport of materials into and out of cells
(Nelson and Cox, 2000). The scientific data also shows that receptors
also respond to electric fields (Adey, 1993a).
Enzymes and membrane receptors, like all proteins, are folded
into 3-dimensional structures. The three-dimensional structure
of a protein arises because each protein is composed of a unique
ordered sequence of amino acids. The proteins of human cells are
all made of chiral molecules called L-amino acids (Nelson and
Cox, 2000).
The location and sequence of amino acids, the location and sequence
of negative and positive charges, and the interaction of the protein
with water and other biological molecules determines the three-dimensional
structure of a protein at body pH (Grattarola et al., 1998; Nelson
and Cox, 2000).
Linus Pauling was the first scientist to discover that specific
sequences of amino acids in a protein can cause it to coil or
wind itself and then take on a helical shape called an alpha-helix
(Pauling, 1988). This structure is particularly prominent in proteins
that are embedded in cell membranes (Nelson and Cox, 2000). In
electrical terms coils and helices are inductors, transducers
and antennas.
The coil-to-helix transition is a nonlinear phenomenon (Grattarola
et al., 1998), which means that it can be triggered by absolutely
miniscule amounts of energy.
The coil-to-helix transition is a cooperative phenomenon called
a two-state function, which is characteristic of any type of electronic
or biological device appropriate for information processing (Grattarola
et al., 1998).
Enzymes and receptors are types of proteins that possess the
ability to fluctuate back and forth between active and inactive
states much like electrical switches that can either be set to
an on or off positions. This cyclical movement between the active
position and the rest position of these types of proteins involves
a reversible shift in the distribution of electrical charges,
which subsequently alters the 3-dimensional folding and chemical
binding sites of these proteins. This alteration in protein folding,
called a configurational or conformational change is accompanied
by changes in both the chemical reactivity and the electrical
properties of these proteins (Wuddel and Apell, 1995).
For many years biologists have recognized that the triggering
mechanism that turns on enzymes and receptors causing them to
transition between their active and rest states involves chemical
interactions where chemical compounds transfer electrical charges
between one another. However, new research has now proven that
the transfer of electric charges does not always require a chemical
carrier. In fact enzymes and receptors can also be activated by
electric charges directly transferred from resonantly coupled
electric fields (Derényi and Astumian, 1998). This is because
the intramolecular charge transfer that occurs in enzymes and
receptors undergoing conformational transitions within their cycle
conveys to these molecules the ability to transduce energy directly
from oscillating electric fields (Astumian et al., 1989).
A number of researchers, especially Ross Adey, have shown that
weak electromagnetic fields may resonantly interact with the glycoproteins
of the cell membrane acting like first messenger signals that
activate intracellular enzymes (Adey, 1993b). These electromagnetic
signals can create conformational changes in cell membrane proteins
when these membrane proteins transductively couple with electromagnetic
frequencies provided the frequencies are within certain amplitude
and frequency windows (Adey, 1993b). This means the cell membrane
proteins can act like electrical transducers that behave as on
off electrical switches that activate chemical processes inside
of the cell (Adey, 1980, 1981, 1988, 1993b; Adey et al., 1982).
"The essential molecular functions appear in fact to be
determined by electromagnetic mechanisms. A possible role of molecular
structures would be the carrying of electric charges, which generate,
in the aqueous environment, a field specific to each molecule.
Those exhibiting such coresonating or opposed fields ("electroconformational
coupling") could thus communicate, even at a distance (Benveniste,
1993)."
For example, it is well recognized by biologists that cell enzymes
such as Na, K-ATPases require energy to pump ions such as sodium
and potassium across cell membranes. However, new data shows that
these enzymes can either be activated by chemical energy derived
from ATP or by energy directly absorbed from electric fields (Xie
et al., 1997). In this case energy from the electric field substitutes
for the energy normally provided chemically by ATP (Derényi
and Astumian, 1998). Any electromagnetic effect on a chemically
based biological reaction in the body is dependent upon the electric
or magnetic frequency sensitivity of the rate constant of the
enzyme involved in the chemical reaction (Weaver et al., 2000).
Membrane receptor proteins can also be activated by resonantly
coupling to electric fields (Astumian and Robertson, 1989).
"If fields can affect enzymes and cells, [one should expect]
to be able to tailor a waveform as a therapeutic agent in much
the same way as one now modulates chemical structures to obtain
pharmacological selectivity and perhaps withhold many of the side-effects
common to pharmaceutical substances (Davey and Kell, 1990)."
The key step necessary for this mechanism to work is to produce
an electric field in the body, which exactly matches the resonant
frequency of the enzymatic process or membrane receptor that you
wish to stimulate so that the enzyme or receptor is able to resonantly
couple to the field. This is exactly how LifeWave LIFEWAVE patches
work.
For
More Info about Our Exciting LifeWave
Patches - Please Click Here!!
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