Istraživačke studije

Featured Article
The Nobel Prize in Chemistry 2003—what are the implications of these new discoveries for BICOM therapy

By: Dipl. Ing. Dr. techn. Horst Felsch, Chemist, Fieberbrunn, Austria


Two American researchers received the Nobel Prize for chemistry in October 2003:
Peter Agre of Johns Hopkins University in Baltimore for discovering water channels in the cell wall, and
Roderick MacKinnon of Rockefeller University in New York for structural and mechanistic studies of potassium ion channels.

The Royal Swedish Academy of Science praised Peter Agre’s work stating:
“This decisive discovery opened the door to a whole series of biochemical, physiological and genetic studies of water channels in bacteria, plants and mammals. Today researchers can follow in detail a water molecule on its way through the cell membrane and understand why only water, not other small molecules, can pass.”

Peter Agre
Fig. 1 Roderick MacKinnon
Fig. 2 Roderick MacKinnon was awarded the Nobel Prize for his work on the way potassium ion channels work. These ion channels are structured differently from the water channels discovered by Peter Agre.

A Nobel Prize had already been awarded in this field back in 1909 to Wilhelm Ostwald who suspected as early as 1890 that signals measured in tissues were a clue that ions were transported in the cell membrane.

A further Nobel Prize received by two British doctors in 1964 indicates the significance of this area of research. They were able to furnish proof of ionic flow in nerve cells.

However, it was not until 1988 that the spatial structure of ion channels was portrayed in three dimensions by Roderick MacKinnon.

François Diederich, head of the Department of Chemistry and Applied Biosciences at the respected Swiss Federal Institute of Technology aptly expressed how far-reaching and revolutionary these discoveries are when he declared: “Roderick MacKinnon has amazed the entire scientific community with his work!”


Fig. 3 Cross-section through a human cell
Our bodies consist of millions of tiny cells. Although these cells may differ considerably in their function and structure, they have one thing in common: their contents are protected by an extremely effective weapon, the cell membrane’s so-called double lipid layer.

Fig. 4 Diagram of the cell membrane with its double lipid layer.
Proteins with different functions are integrated in the cell membrane.

What is this?
To put it simply, each cell is surrounded by a paper-thin fatty layer, 7 – 10 nm thick (1 nm = nanometre is one millionth of a millimetre).

The proportion made up by this fatty layer varies according to the cell’s function: for example, the cell membrane of the human blood cell contains 43% lipids. In nerve cells it is as much as 76%. Mitochondria, which are responsible for intracellular energy metabolism and consequently have a particularly important role to play, even protect themselves with two membranes, the cell membrane and the mitochondrial membrane which is only 24% fat, however.

It can be concluded from this that the higher the proportion of fat in the cell membrane, the better protected the cell.

Yet, despite its fatty layer, this cell membrane cannot be completely impermeable as the cell needs to be nourished and supplied. For this, substances have to be exchanged through this membrane.

The concentration of sodium and potassium ions must also be kept in balance so that the necessary membrane potential, and consequently the functioning of the cell, can be maintained.


How can water or particles dissolved in water (ions) pass through a water-repellent fatty layer into the interior of the cell?

A physiology textbook explained back in 1980 that water is transported into the intracellular space by osmotic forces.

This assumption does not explain, however, why water molecules penetrate the interior of the cell extraordinarily quickly. Measurements taken in the 1950s revealed that 2 billion water molecules were carried per second and channel and, based on the size of the channel, water molecule flow rate was calculated at 5 metres per second.

It is impossible to achieve speeds such as this purely through osmotic processes and they are also inconceivable from an energetic point of view.
It was already being postulated back in the mid 19th century that the membrane shell must contain openings for substances to be exchanged.

In the early 1980s Peter Agre was investigating water transport mechanisms in red blood cells and in 1988 isolated a previously unknown protein which is responsible for this transport: Aquaporin AQP.

Amongst other things, this aquaporin regulates the water balance in the kidneys, the red blood cells, the eye lens and the brain.

Dysfunction leads to diabetes, grey cataracts and neuronally induced loss of hearing.

It is obvious from the microscopic size of these water channels why they could not be detected with normal light microscopes: the diameter measures around 0.3 millionth of a millimetre = 0.3 nm, the length 1 millionth of a millimetre = 1 nm.

High-resolution electron microscopes were needed to make such small dimensions visible.

Fig. 5 Water channel in the cell membrane. The individual water molecules are guided through at high speed helped by the aquaporin protein strand (depicted as a spiral).


A channel intended for transporting water inside the cell measures 0.3 nm in diameter. The tetrahedron-shaped water molecule also has a diameter of just under 0.3 nm. In other words: only individual water molecules can pass along this channel, but no water clusters!

Fig. 6 At a wave number of 3,400 cm–1, the infrared spectrum of liquid water displays a broad OH band caused by the hydrogen bridge-type bonds of the water cluster.

This fact has caused the thinking behind water research to be revised and has also thrown up a number of questions.

As a dipole, the water molecule forms hydrogen bridge-type bonds and combines with other water molecules to form a water cluster.

This idea is correct and is also confirmed by pictures of liquid water taken using infrared spectral photometry.

If only single molecules can pass through a water channel, does this water cluster have to be re-formed into individual molecules before being transported through the cell membrane?

The answer is clear: yes.

This immediately leads to further questions.

Is the information conveyed by the water actually stored in the special structure of the water cluster? – homeopathy confirms this.

Is this information lost when the cluster is broken up at the surface of the cell and is the original information available again after the molecules are transported individually through the water channel into the interior of the cell?

This new knowledge has also changed some of my thinking too.

In May 2003 (in other words, before the announcement of the Nobel Prize for chemistry) I wrote the following with regard to ion channels on page 7 of the proceedings to the 43rd Congress for BICOM users:

We know that the cell membrane does not allow any ions to pass through its double lipid layer. This would consume too much energy. To allow ions to be transported passively, cell membranes have so-called ion channels for sodium, potassium, magnesium, calcium and chloride ions.

These ion channels are a specific size and also selective, i.e. they allow only the named ions together with their hydration sheaths through.

According to the research results of the two Nobel Prize winners, both the water channels and the ion channels are too narrow to allow whole water clusters or ions together with their hydration sheaths to pass through. Only individual molecules (e.g. water) or ions without hydration sheaths are transported.

I shall deal with the resulting new knowledge on information transfer through the water channels a little later in the text.


First to Roderick MacKinnon.
It is fascinating to read in his publication how he demonstrated the high selectivity of ion channels through the example of the potassium ion channel.

Fig. 7 A potassium ion channel
At the point of entry (A) the potassium ion is still hydrated with water molecules. These are cast off so that the ion migrates “naked” through the selective channel. Spiral-shaped proteins take care of transport. Shortly afterwards hydration occurs again. A locking mechanism ensures the necessary membrane potential.

Thus the much smaller sodium ion, for example, is not transported through this channel.

The larger potassium ion, on the other hand, is carried virtually “by hand” though this channel.

These “hands” are polarised oxygen atoms, also present in the hydration sheath of the potassium ion.


If a sodium salt (e.g. sodium chloride, NaCl) is dissolved in water, the polarised water molecules penetrate the lattice structure of the solid salt and break up the lattice bonds to the sodium and chloride. Positively charged sodium ions and negatively charged chloride ions are formed as a result.

The next step is the hydration of the two ions. The negatively charged oxygen atoms in the water molecules dock with the surface of the sodium ion and form a sodium-specific hydration sheath through hydrogen bridge-type bonds. This sheath contains the information: “I am a sodium ion.”

A similar thing happens with the chloride ion. As it is negatively charged, the positively charged hydrogen atoms in the water molecule dock with its surface, likewise forming a chloride-specific hydration sheath.

This hydration process produces a gain in energy and is also consequently completed fully at great speed by the “solvent water”.


How does a hydrated potassium ion differ from a sodium ion which is also hydrated?

The differences in size which were discussed earlier are not a selectivity criterion for the ion channels!

What is then?
It is the number of docking points for water molecules on the surface of the ions.

Let me explain.
The hydration number of an ion indicates how many water molecules can dock with its surface. For the potassium ion it is 4, for the sodium ion it is 8 molecules, so a marked difference!

Now to the details.
With the potassium ion, therefore, up to 4 water molecules can adhere to the surface through the negatively charged oxygen atom, i.e. there are 4 adhesion points. The coherence between ion and oxygen atom occurs through so-called van der Waals forces.

If these 4 water molecules have attached themselves to the potassium ion, the potassium-specific water cluster can be built up through hydrogen bridge-type bonds.

What is new about this knowledge is the all important adhesion points – in other words, the foundations on which the cluster structure develops. In the past it had been assumed that the specificity of the information lay in the actual cluster. Now it is known that it comes from the adhesion points.

Fig. 8 Detailed illustration of potassium
ion channel
4 water molecules dock with the potassium ion to build up the hydration sheath (top picture). In the potassium ion channel these 4 bonding arms are also formed by oxygen atoms (bottom picture) which are bonded with proteins however. This prevents information being lost and ensures high selectivity.

And now it gets interesting.
These four docking points on the surface of the potassium ion are also found in the potassium ion channel. As the potassium ion with its huge water cluster is too large for the specific potassium ion channel, the water cluster is cast off at the surface of the cell.

In the ion channel itself there are also negatively charged oxygen atoms (bound to channel protein) which grab onto the four docking points which are free now that the water cluster has been cast off. The potassium ion is identified and actively transported at great speed through the potassium channel – as if carried by hand.

In contrast, the sodium ion needs 8 “arms” to be transported through the ion channel (hydration number 8). However, the large potassium channel can only provide 4 arms, i.e. it is 4 arms short. The potassium channel consequently realises: you aren’t a potassium ion. Therefore the hydrated sodium ion cannot cast off its hydration sheath and also cannot migrate through the potassium channel since, with its hydration sheath, it is far too large.

It is important to answer one more question, however.
If the potassium ion casts off its hydration sheath because it is too large to pass through the potassium ion channel, an energy source must make this process possible. Just to recap: energy is gained in hydration. This is needed again when the water sheath is cast off!

Roderick MacKinnon was able to demonstrate, however, that casting off the hydration sheath and the “naked” potassium ion docking with the four oxygen contact points in the ion channel does not produce energy flow.

Once the potassium ion has passed through the ion channel, it is immediately hydrated inside the cell and reverts to the original state it was in outside the cell.


The specific information e.g. “I am a potassium ion” comes from the docking points on the surface of an ion. These docking points are also the basis for the ion-specific structure of the hydration sheath which forms around all ions.

So this specific information is not found somewhere in the middle of the huge hydration sheath which envelops an ion; it comes from a design which all ions carry on their surface.

The docking points on the water molecule are the foundations of this design. Consequently the remainder of the hydration sheath structure is already pre-determined architecturally – or to be more accurate – in its informative composition.

In the past it was believed that, when an ion lost its hydration sheath, ion-specific information was lost with it.

It is now known that an ion can cast off its hydration sheath without losing information if the docking points on the ion surface are taken over by negatively charged oxygen atoms sitting on the surface of a protein molecule, for example.

Where pure water is transported through the water channels this protein is called aquaporin.

These new discoveries have also improved understanding of the efficacy of homeopathically diluted substances.

If the central ion is no longer present in high dilutions, the energy introduced with the potentisation movement ensures that the former adhesion points of the negatively charged oxygen atom on the ion surface remain structurally intact. Consequently the design of the hydration sheath and also the information stored within it remains unchanged.

While, in the past, it was believed that the ion’s specific information was contained in its water cluster and this was therefore the actual information centre for the cell, this can now be expressed more accurately. The information centre is the docking points of the hydration sheath on the surface of the ion.

In the past it was believed that a hydrated ion transferred its information to the cell by feeling the external structure of the hydration sheath all over.

It is now known that the ion casts off this hydration sheath completely, i.e. the entire hydrate structure is torn down to the ground. The water cluster’s docking points on the ion surface are thus the actual information code which the ion does not lose even when it migrates through the ion channels.


The 2003 Nobel Prize winners for chemistry have shown us how water and ions are specifically transported through the cell membrane.

This transporting of substances is vitally important for the cell’s functioning. Membrane potential is built up through ion transport. This, in turn, is a requirement of the cell’s excitability and thus for it to function.

Isn’t it fascinating that millions of cells work together smoothly in a healthy body. But how do they exchange information?

Prof. Popp drew a highly memorable comparison here: cells are like tuning forks. Perfect harmony results in a healthy body. Diseased cells lead to dissonance and upset this harmony.

Bioresonance therapy receives the “full concert” created by the oscillating cells via the input electrode. The BICOM device is able to filter out dissonance, strengthen the “chorus of healthy cells” and return it to the body. In this way the diseased cells receive the energy they need to oscillate harmoniously again.

Back in 1931 GEORGES LAKHOVSKY spoke of the cells’ vibrational equilibrium.

Peter Agre and Roderick MacKinnon’s work shows in an impressive fashion how information is built up in the body and how it is passed on without loss of energy. Unimpeded information flow is obviously extremely important to the body.

If this is the case, then the question of why cellular information is so little used in therapy is totally justified.

In his book “Wasser und Information” [Water and information] which appeared in 1993, Prof. Hans Leopold of the Institute for Electronics at Graz Technical University stated the following:

“Intervention is more skilled and thus more targeted, firstly if the code is known and secondly if an information intersection is found through which information from outside can be brought into the living system. [Note: The two Nobel Prize winners deciphered this!] In my opinion, these two aspects I have just mentioned are very important for new (or old rediscovered) methods in medicine.”

Bioresonance therapy uses information from the body as a therapeutic approach. It therefore pursues “new methods of great importance in medicine.”

The scientific discoveries of the two Nobel Prize winners confirm that metabolic processes are always linked with the transmission of information. Therefore, conversely, it must also be possible to restore balance to impaired metabolic processes by transmitting the “correct” information.

BICOM resonance therapy has been confirming this for over twenty years through countless cases of successful therapy.


Prijatelji Centra