Ionising HHO with Ozone generator

Stanley Meyer 1992 Interview

Cold Fusion: Fire From Water

FUKAI hydrogen energy from Japan

This technology can be used to generate hydrogen simply by adding either aluminum or magnesium to functional water.
Two liters of hydrogen can be generated for each gram of aluminum, while each gram of magnesium will generate 3.3 liters of hydrogen.
This will allow the production of 1kwh of electricity at a low cost of approximately 15 yen (calculated based on the use of unused aluminum powder).
This cost can be reduced even further by using recycled aluminum cans.

The experiment in the following video shows how quickly and easily hydrogen can be generated with this technology.
Functional water allows hydrogen to be generated in large volumes.
The bonds of hydrogen molecules in functional water are easily broken, and the reaction with either aluminum or magnesium produces a large volume of hydrogen.
Functional water is produced by simply passing tap water through an apparatus that contains natural minerals.
Elaborate facilities and laboratories are not required.

Since functional water can be produced simply by passing tap water through an apparatus that contains natural minerals, there is no energy cost.

"If we use this technology in the future, we will be able to drive cars without gasoline or electricity, using only water.
Water will become an energy resource, replacing petroleum-based fuel.
We are currently researching and developing technology to generate hydrogen at zero cost.
Someday it will be possible for each household to generate its own hydrogen. The private generation of electricity using hydrogen is not an impossible dream."

The Rainbow Ensemble

ISIS Report 20/10/10 
Water’s Quantum Jazz

The Rainbow Ensemble
##################

How water keeps ‘most everything in the cell dancing most of the time, and 
what’s the cell really like. Dr. Mae-Wan Ho

We are now ready to venture inside the cell and see how everything, the rainbow 
ensemble, can do water’s quantum jazz together. We start by considering the 
interaction of water with ions and proteins.

Salt out only if you must 

The interaction of charged ions with water and proteins is at the heart of many 
signal transduction processes in the cell. Enzymes and cofactors are highly 
specific in their requirements for metal ions; while the addition of a phosphate 
group to proteins and metabolites – phosphorylation - are widely involved in 
activating enzyme pathways of biosynthesis and energy metabolism. What is the 
origin of these ion-specific effects? At a more fundamental level, why do 
different salts vary so much in solubility? And why do some salts precipitate 
proteins from solution more so than others?      

Numerous studies have confirmed that small ions of high charge density are 
kosmotropes (order inducing) and bind water molecules strongly; while large ions 
of low charge density are chaotropes (disorder inducing) and bind water 
molecules weakly relative to the strength with which water molecules form 
hydrogen bonds with one another (see [1] Dancing with Ions, SiS 48). Kosmotropes 
tend to attract a solvation shell with more water molecules, while chaotropes 
have small solvation shells with less water molecules. But that is only half the 
story. The other half of the story begins with how ions interact with proteins.

Franz Hofmeister, a Czech scientist in the late 19th century, found that some 
salts helped egg white proteins to dissolve in water, while others caused the 
proteins to precipitate out, and there were those that had effects in between. 
He ranked the ions according to their ability to “salt-out” and “salt-in”, which 
resulted in the Hofmeister series. The Hofmeister series is also correlated with 
the ability of the ions to induce protein unfolding, coalescence of bubbles and 
many other phenomena, though there has never been a satisfactory explanation 
[2].

Kim Collins at University of Maryland Medical School, Baltimore, USA, may have 
found the answer [3, 4], and it is related to the ions’ affinity for water. 

When pairs of oppositely charged ions have similar affinities for water, 
something special happens: they come out of their solvation shells, join up and 
neutralize each other. That’s because they can just as easily form intimate 
partners with each other as with water molecules; exchanging water molecules for 
the counter-ion does not cost anything in energetic terms. This ‘Law of Matching 
Water Affinities’ appears to explain why certain salts are less soluble than 
others, and why some salts precipitate proteins out of solution while others 
help them dissolve. The answer is that only neutral molecules precipitate (or 
crystallize) out of solution; neutral molecules have much lower solubility. 

More specifically, according to Collins, a radius of 1.06 ? separates small 
monovalent cations from large ones, and a radius of 1.78 ? separates small 
monovalent anions from large ones. Small monovalent ions are strongly hydrated, 
while large monovalent ions are weakly hydrated (see Fig. 1). For example, LiF 
contains small monovalent ions that readily come out of their hydration shells 
to pair up as ‘contact ion pairs’, it has a solubility of only 0.1 M. In 
contrast, CsF has a large cation and a small anion, and do not pair up in 
solution; it has a solubility of 24.2 M.

Figure 1  Monovalent kosmotropes & chaotropes ordered by size; the size of their 
hydrated ion is in inverse order

Proteins have strong negatively charged carboxylate groups (COO-) on their side 
chains that pair up well with kosmotrope cations, so Na+ salts out proteins, 
while a chaotrope such as Cs+ salts them in. Similarly, Ca2+ is well-matched to 
carboxylate in water affinity and will also salt out proteins. 

Read the rest of this article here
http://www.i-sis.org.uk/theRainbowEnsemble.php

This is the fourth article in the series Water’s Quantum Jazz

Fast Freddy Update

Water Is The New Oil