**RIFE
FREQUENCY GENERATOR: **

**THE PHYSICAL STRUCTURE OF
VIRUSES AND BACTERIA, WHICH MAKE THEM EXTREMELY SUSCEPTIBLE TO DESTRUCTION BY
SPECIFIC STRUCTURAL RESONANT MECHANICAL VIBRATIONS**

**By Gary Wade, Physicist:
APPENDIX D**

**Dr. Royal Raymond
Rife in his research as shown In Appendix A, was able in 1920 to build the
first of five optical microscopes, which were able to overcome the normally
found Fraunhofer diffraction limitations to size resolution occurring in
today's commonly used optical microscopes. Rife's microscopes were able to see
viruses! In Appendix B it was shown how Rife, while observing with his
microscope, used his frequency instrument to destroy viruses and bacteria. It
was also alluded to it being some sort of resonant vibrations set up in the microbe
structure by the frequency instrument that destroyed the microbe. In Appendix C
an example of a simple virus capsid ( protein coat ) was used to show how
structural resonance vibrations can destroy a virus. In this Appendix D a
detailed look at the physical structure of virus capsids will show that they
have construction which is particularly susceptible to destruction by
structural resonant vibrations. Also a look at bacteria cell membrane and
bacteria cell wall structure will suggest how and why bacteria are also
susceptible to destruction by exposure to structural resonant vibrations.**

The study of virus
types and structure is a very complex endeavor. (Ed: Even if you are a layman,
this is worth the effort, but you may want to start with some of the less
technical articles such as** RIFE
THERAPY MADE SIMPLE)** In this Appendix we will only consider
simple virus capsid structures in detail. However, these simple virus capsid
structures will have structure patterns which are common to all viruses and
will illustrate why all viruses are susceptible to destruction by structural
resonant vibrations. Almost all viruses of interest can be classified under two
headings: 1) Viruses with helical symmetry, and 2) Viruses with icosahedral
symmetry.

Two viruses with
helical symmetry are illustrated in Figures 1 and 2 and will serve as prototypes of the viruses of
helical symmetry. Figure 1 illustrates a segment of the well known tobacco
mosaic virus. In this virus, identical protein molecules associate with the
virus RNA genome to form a right handed helix pattern as shown. This assembled
virus is also called a naked helical nucleocapsid. Naked because there is no
lipid bilayer coat around the helical nucleocapsid. When ever the genome of a
virus is enclosed by a protein coat it is called a nucleocapsid**.** Figure 2 illustrates a helical nucleocapsid strand which has been wound
into a still much larger helix, which is encapsulated in a lipid bilayer
envelop membrane, which has glycoprotein spikes on its outer surface. The
tobacco mosaic virus structure is typical of many viruses that cause plant
diseases. The virus structure illustrated in Figure 2 is typical of many
viruses that cause animal/human diseases. For example, influenza and measles
viruses. We will see later on in this appendix that viruses with helical
symmetry can be treated as torsional oscillators and by over driving these
torsional oscillators at their resonant frequency they can be destroyed.
However, first we will study the protein coat ( capsid ) structure of the by
far most common and numerous types of viruses to cause diseases in plants and
animals. Namely, viruses with icosahedral symmetry.

Illustrated in
Figure 3A,B, and C** **are three different views of
a icosahedron. The icosahedron has 20 equilateral triangle faces, 12pt vertices,
and 30 edges. The opposing vertices lay on an axis of five fold symmetry as
illustrated in Figure 3A. In other words each time the icosahedron is rotated (
720 = 3600 /5 ) about one of these six axes it is brought back into the same
state. The axes through the centers of opposing equilateral triangles have
3-fold symmetry as illustrated in Figure 3B. In other words each time the icosahedron is rotated ( 12pt00 =
3600 /3 ) about one of these 10 axes it is brought back into the same state.
The 15 axes through the centers of opposing edges are axes of 2-fold symmetry,
as illustrated in Figure 3C. In other words each time the icosahedron is
rotated ( 1800 = 3600 /2 ) about one of these 15 axes it is brought back into
the same state**. **Figure 4A and B illustrate how a section of an isometric net can be
folded into an icosahedron. Such an isometric net for constructing icosahedrons
is illustrated in Figure 5. Figure 5A shows the isometric net section of Figure
4A. Now it is an amazing fact that most viruses have capsids surrounding the
viral genome, which have icosahedral symmetry. It is this fact of icosahedral
symmetry of the capsid that allows us to associate a repeating protein pattern
with the specific isometric net illustrated in Figure 5, from which a virus
capsid can be constructed by the method illustrated in Figure 4A. The circles
in Figures 5B,C,D,E, and F represent protein molecules. You can imagine
isometric nets in which each of the protein molecule patterns of Figures
5B,C,D,E, and F each fill the entire isometric net. Then by removing an
isometric net segment as illustrated in Figure 5A from each of these isometric
nets, five different virus capsids can be constructed. It should be noted that
even though I have shown identical circles implying identical protein molecules
in each of the isometric nets, in fact most viruses use two or more different
protein molecules in their capsid. So just think of the circles as place
holders for different protein molecules.

Do to the high symmetry
of the specific isometric net of Figure 5, which produces icosahedral symmetry,
it is possible to chose isometric net sections, which have the same shape and
symmetry as the isometric net section of Figure 5A, but consists of integer multiples of the 20 unit triangles of
Figure 5A. These larger isometric net sections can of course also be folded
into an icosahedral shape, but are properly called deltahedra. Some of these
possible deltahedrals are illustrated in Figure 6. Figure 7 illustrates some of the possible equilateral triangular
deltahedral faces, some of which were illustrated in Figure 6. For a simple
concrete example consider Figure 8. In Figure 8 we have constructed an isometric net
as was suggested in Figure 5C. In Figure 8, three equilateral triangular (
protein ) faces are illustrated, namely triangles ABE, ACF, and ADG. These
triangle faces are illustrated in virus capsid models you are going to
construct, from Figures 9A,9B, and 9C respectfully. These are all simple examples of
deltahedrals illustrated in Figure 6A. Now looking back at Figures 3D,E, and F we see spherical or inflated versions of Figures 3A,B, and C respectively. The inflated versions have the exact
same 5,3,2 rotational symmetry as the icosahedra and can be constructed from
the same stretched or deformed isometric net as the icosahedra was. The
importance of this is that viruses with icosahedral symmetry are generally
spherical in living tissue due to hydrophilic interaction between virus coat
proteins and or lipid bilayer with tissue water and osmotic pressure.

Figures 9A,B,C,D,E,F,G, and H are all simple virus capsids for you to
construct. The importance in constructing these capsid models is, that until
you construct them, you are not likely to clearly see just how highly symmetric
, over lapping, and closed on its self these periodic protein clump patterns on
virus capsids are. The importance of this high symmetry, over lapping, and
closed on its self periodicity is that it makes each virus type exceedingly
easy to destroy with its own specific frequencies of mechanical structural
resonance vibrations.

Here are the
instructions for assembly of the virus coat in Figures 9A,B,C,D,E,F,G, and H.
First go to a copy machine and enlarge the figure 12pt2% two times. This will give
almost a page full of virus coat. Second, make another copy of the last
enlargement onto thick cardboard copy paper. You may have to look around to
find the right copy machine for this. Third, cut out all dashed lines on the
cardboard copy. You should now have something that looks like Figure 4A except for extra tabs for gluing the model together. ( I have
found that Elmer's Glue All works well ). Fourth , taking a straight edge ruler
and lining its edge up congruent with all of the equilateral triangle facet
edges as those shown in Figure 4A, fold the cardboard over the ruler edge until
a 90 degree fold angle is achieved, while folding away from the faces shown in Figures 9A through 9H. Be sure to fold all of the glue tabs this way
also. Fifth, begin gluing adjacent tabs flush together. It may prove helpful to
use scotch tape to tape the adjacent faces together after gluing while waiting
for the glue to set. Also strong alligator clips are useful in holding the
glued tabs together while the glue sets up. Have fun and may the glue be with
you.

Once you have
several virus capsid models constructed, you will observe numerous closed rings
of protein molecules ( clumps ) as illustrated in Figure 10 or as directly visible in the plant virus capsids illustrated
in Figure 11. These closed periodically spaced protein
clump rings form a pathway for mechanical wave motion. In fact they are a
biological manifestation of the classical physics problem of wave motion on a
periodically spaced mass beads on an elastic string with circular boundary
conditions. The solutions to the problem are the well known quantatized
standing wave solutions. For each quantatized wavelength solution there are two
transverse oscillation modes for the system ( closed ring ) and one longitudinal
oscillation mode. There is a total number of independent oscillation modes
equal to three times the number of masses in the closed ring. Looking at Figure 10, one transverse mode would be protein molecules (clumps) being
alternately displaced above and below the plane of the page. The other
transverse oscillation mode for the same particular wavelength solution would
be at right angles to this other mode. It would consist of the alternate displacement
of the same protein clumps toward and away from the center of the closed ring
of protein clumps. The longitudinal mode consists of protein clumps being
displaced back and forth about their equilibrium position along the arc length
of the ring. All three modes are allowed to exist simultaneously. Figure 12ptA shows a mathematical abstraction of a closed
ring of ten protein molecules ( clumps ). Figure 12ptB shows the same ring
linearized and extended in length for graphical purposes to easily illustrate
standing wave motion. Figures 12ptC,D, and E, show the transverse and or
longitudinal displacement patterns associated with some of the standing wave
solutions for the ring. Similar displacement patterns can be drawn for other
closed rings with various numbers of protein clumps per ring. For example
Figure 12pt F and G illustrate the standing wave pattern for a ring consisting of
five protein molecules. What is crucial to note is that some standing wave
displacement patterns put far more stress on the ring than others.

The most stressful
standing wave displacement pattern is one where adjacent protein molecules (
clumps ) oscillate 180 degrees out of phase as illustrated in Figure 12ptC. This
mode places maximum stress on the relatively weak adjoining bonds between these
protein clumps. If the displacement amplitude becomes to large the bonds will
rupture and the ring will disintegrate. Now examining the various capsid models
you have constructed, you will note these ring patterns are commonly
overlapping and or tangentially bonded to each other. For example the capsid
constructed from Figure 9C has how many: 1) Rings with five member protein
clumps, 2) Rings with six member protein clumps, 3) Rings with ten member
protein clumps, and 4) Rings with fifteen member protein clumps? How many of
the five member rings overlap with each other? How many of the five member
rings are tangential to each other? With how many other six member rings does
each six member ring overlap or intersect? With how many other ten member rings
does each ten member ring overlap or intersect? With how many other fifteen
member rings does each fifteen member ring overlap or intersect? Now how do all
of the rings overlap or intersect with each other? By now you should have had a
cathartic experience realizing just how cross coupled even a very simple virus
capsid is when considered as a reservoir for standing wave energy. Now realize
that at each overlap or intersection region for each protein molecule in the
rings discussed above, the bond strength is relatively very weak and that
combined random mixing of standing wave displacement amplitudes from even ultra
low intensity ( ~10-16 w/m2 ) standing waves on the various rings can rupture
these bonding regions. When Rife exposed viruses to their most stressful
mechanical oscillation mode, he could literally while viewing them through his
microscope, see them disintegrate and or even explode. And as was shown in
Appendix B, Rife was only using ultrasound intensity levels of around 10-16
w/m2 .

So far we have
avoided the use of mathematics and differential equations to illustrate
standing wave motion on the virus protein coat ( capsid ). However, to fully
appreciate how and why a virus is so susceptible to its own mechanical
structural resonant vibration frequency it is necessary to apply some simple
physics to the problem. All the physics that will be used is readily available
in undergraduate physics mechanics text books, so I will simply state the
results here. Figure 13A illustrates a ten member protein clump ring
such as we have found in virus capsids. Figure 13B is the mathematical
abstraction of Figure 13A. Figure 13C focuses in on the oscillation of a single
protein clump of the ring while it is executing a single mode oscillation of
the most stressful oscillation mode to bonds in the ring. ( The results we will
obtain are however valid for all oscillation modes. ) The differential equation
of motion for free oscillation of the system shown in Figure 13C is equation 1.

Equation 1

d2S/dt2 + ( b/m )
dS/dt + Wo2 S = 0 ,

where S is
displacement of the center of mass from its equilibrium position, m is the mass
of the protein molecule, b is a positive drag factor constant, and Wo is the
natural resonance angular frequency of the system. If the mass m of the system
is displaced a distance So from its equilibrium position and then released to
perform free oscillation* , a situation as depicted in Figure 14 will then
occur. This is the graphical representation of the solution to equation 1. Figure 14 shows that the amplitude of oscillation
decreases exponentially with time due to the velocity dependent drag force. The
strength of the drag force is represented by the magnitude of b. A useful
quantity when discussing oscillating mass systems is the Q-value defined as:

Equation 2.

Q = (Wo m )/b ,

When the Q-value is
large ( relatively small b ) , as it is for the oscillating mass system
depicted in Figure 14, then the average power (Pd) radiated or dissipated by
the oscillating system per oscillation cycle is given approximately by:

Equation 3,

Pd = E(Wo/Q) ,

where E is the
total energy of the oscillating system at the time of interest. For our system
almost all power is dissipated in the form of pressure waves in the fluid
medium in which the virus is maintained.

Now if the system
in Figure 13C were to be exposed to a periodic driving
force such as sinusoidal pressure waves, then the differential equation of
motion for the system would be given by:

Equation 4,

d2S/dt2 + (b/m)
dS/dt + Wo2 S = Fo Sin Wt ,

where Fo is a
constant and the maximum amplitude of the driving force (Fo Sin Wt).

The steady state
solution to equation 4 is:

Equation 5,

S = B Cos ( Wt -
& ) ,

where & is a
phase constant and B is given by :

Equation 6.

B = (Fo)/( m2( Wo2
- W2 )2 + W2b2 )1/2 .

Figure 15 shows B plotted against the angular
frequency of the driving force for the case where the mass and the peak value
of the driving force are held constant while the drag force is allowed to vary.
Note the horizontal dashed line that intercepts the curve for b = bo. Let the
displacement value ( oscillation amplitude ) given where the dashed line
intercepts the displacement axis be the displacement value which corresponds to
the oscillator self destruction ( adjacent protein bonds rupture ). In this
situation Figure 15 would then indicate that for the driving force used, the
protein ring would be ruptured, if b was much smaller then 3bo. Another way to
say this is , if your oscillator has a very small b value, then a very small
driving force can destroy it provided the driving frequency is close enough to
the resonance frequency.

Still another
approach to understanding the oscillator self destruction process is to look at
the power absorption by the oscillator from the driving force. Equation 7 gives
the power absorption (Pa) of the oscillator from the driving force.

Equation 7.

Pa = ( 1/2 FoW2b) /
(m2(W2-Wo2 )2 + W2 b2) ,

Pa is plotted
verses angular frequency in Figure 16 for a constant value of maximum driving
force Fo , constant mass (m), and three values of b. The curve in Figure 16 are
for a situation of dynamic equilibrium. That is power absorption from the
driving force equals power being dissipated by the oscillator. In our case
almost all dissipation is done by re-radiation of the pressure wave, which is
driving the system. Let the dashed line intercept indicate the re-radiation
power level at which the oscillator's amplitude is at the self destruct point.
Any further power absorption and the oscillator will not be able to increase
its amplitude of oscillation because it will come apart (rupture). Figure 16
illustrates that if your oscillator has a small enough b value, then a very
small driving force can destroy it, provided the driving frequency is close
enough to the resonance frequency ( Wo ).

Let us now return
our attention to viruses with helical symmetry. Close examination of the two
prototype helical viruses of Figures 1 and 2 shows that what we have in
these two viruses is a good analog to an elastic spring. And just like an
elastic spring you will have a natural specific torsional resonance frequency
for each helical virus. For example for a torsional spring oscillation, the
equation of motion is given by:

Equation 8

(I)dS2/dt2 = - CS,

where I is the
moment of inertia of the helical mass about its length axis, S is the angular
displacement from equilibrium ( zero torque ), and C is the torsional stiffness
, a constant. Equation 8 has a solution of:

Equation 9

Wo = (C/I)1/2 ,

If this frequency
of ultrasound is applied to the helical structure with enough intensity the
helix will come apart. It should also be noted that relatively long ( large
length to width ratio ) helical viruses should also be susceptible to damage by
ultrasound frequencies that set up standing longitudinal wave motion along the
virus axis. And particularly the simultaneous application of ultrasound
frequencies for both torsional and longitudinal standing waves should be
particularly destructive to the helical viruses. With the proper choice of
frequencies and relative intensity between frequencies and absolute intensities
we should be able to convert helical viruses into organic trash in one second
or so.

Before taking up
bacterial susceptibility to structural resonant vibrations, let us summarize
what has been learned about destroying and or controlling virus infections
using structural resonant vibrations. Figure 17 illustrates the structure of the supposed
cause of AIDS, the HIV. HIV has three obvious periodic structures that can be
attacked by structural resonant vibrations. First, there are the periodically
placed glycoprotein spikes on the surface. Second, there is the deltahedra
outer capsid. Third, there is the inner capsid. Each of these structures is
destructible by its own structural resonant vibrations. Since the ultrasound
intensity levels of structural resonant vibrations required to destroy a virus
are so ultra low ( 10-16 w/m2 ) , it is practical to keep a person infected
with a virus under continuous exposure to structural resonant vibrations for
that virus. This can be achieved in several ways: 1) The person can ware a
small inconspicuous ultrasound transducer unit ( see Appendix F ), 2) Rife
frequency instrument type "light" can be installed at home or in the
work place, and 3) Structural resonant vibration ultrasound can be carried by
the room air. Now, if the body's immune system is actively hunting for and
destroying cells infected with the virus of interest ( this process can be
stimulated by a vaccine ) and if the virus is not being allowed to infect new
cells do to its destruction by structural resonant vibrations, then the body
can potentially rid its self of the virus completely.

Now on to bacteria
destruction by structural resonant vibrations. From the remnants of Rife's work
still publicly available, it is clear that Rife was able to destroy all
bacteria he encountered using his frequency instrument. In other words he could
just as easily destroy viruses as bacteria with his frequency instrument ( see
Appendix B ) . It is assumed in the first sentence of this paragraph that
bacteria can be destroyed by structural resonant vibration phenomenon, which
are of the same nature as that for virus destruction. I know of no direct
observational proof of that. However, there is good circumstantial evidence for
it. Though the cell wall structure of bacteria in general appears to be a
continuous strong tough uniform material, a closer look at high power with
electron microscopes show that there are numerous pores, surface projections,
such as pili, which are transmembrane and transwall structures as are flagella.
All of these structures have periodic protein clump structures associated with
there construction and or immediate environment. For example, pili protein
subunits( clumps ) are arranged in a regular helical configuration. Which, if
any of the above periodic protein clump structures can be easily disrupted by
structural resonant vibrations is not known at present. Someone or some
institution will need to construct a modernized version of a Rife microscope (
see Appendix A ) and actually observe bacteria cell destruction by a Rife
frequency instrument device to determine where the weak spots are in the
bacteria cell wall which allow osmotic pressure to rupture the bacteria and
spill its contents out.

You should now
understand how Rife, using his frequency instrument, was able by 1939 to
destroy the viral and bacterial pathogens associated with 52 major diseases,
including cancer ( see Appendix G for connection between BX and BY cancer viruses
and the genetics of cancer cells). Rife's results were fully and completely
verified by the 1934, 1935, and 1937 test clinical trials, which were carried
out by the U.S.C. Medical School Special Medical Research Committee, that
oversaw the clinical trials. The responsibility for the deaths of, suffering
by, and the financial ruin of tens upon tens of millions of people since 1937
clearly rests with the cowardly, greedy, and corrupt leadership/ownership of
the medical industry. This includes pharmaceutical and insurance companies
which have been major benefactors and purveyors of the greed and associated
corruption. Rife treatment methods should be available everywhere right now! Of
coarse this would reduce patient suffering and so called health costs in the

In

**IF YOU FOUND THIS ARTICLE OF REAL VALUE, PLEASE MAKE A HARD COPY WHILE STILL AVAILABLE.**

Taken from: DR.RIFE
AND THE DEATH OF THE CANCER INDUSTRY,

a paper by
physicist Gary Wade