Important New Scientist article on water structure and homeopathy!
Posted: Fri May 05, 2006 7:35 pm
Friends...
Below is a fabulous article on the STRUCTURE OF WATER and
HOMEOPATHY...and it is fascinating scientific verification of what those of
us involved in homeopathy may already know...
And one of the co-authors of this important new research is IRIS BELL,
MD, PHD...who is the head of research for Dr. Andrew Weil's Program in
Integrative Medicine at the University of Arizona. Iris is a HOMEOPATH, and
she has published some great research on homeopathy...she discussed her and
other important work at the NCH Conference a couple of weeks ago...and
H.E.S. (www.homeopathic.com) has just begun to sell the set of CD-audios for
the day-long workshop in which she spoke...she was BRILLIANT!
By the way...I just spoke at Stanford Medical School this week, and
there was a lot of interest in this subject when I mentioned this new work.
I'm giving two talks at UCSF's School of Medicine next week, and I cannot
wait to present this information to them. Basically, anyone who says that
there is nothing in "homeopathic water" are simply uninformed about the
nature of water (no surprise here!).
--Dana Ullman
New Scientist 8 April 2006
The Quantum Elixir
Water. It's the foundation of life on Earth. But what is it about H2O that
gives it this amazing ability, asks Robert Mathews
IN NEW AGE circles, everyone is talking about it: the magical properties of
the colourless, tasteless liquid the rest of us blithely refer to as water.
Between frequent gulps of the life-giving elixir, those initiated into its
secrets talk reverently of the work of Masaru Emoto, who is said to have
proved that water responds to the emotions of those around it. They describe
how Emoto has demonstrated that ice crystals made from water blessed by a
Zen monk look so much more beautiful than those exposed to messages of hate.
Many have bought his best-selling book detailing his findings, and many more
have seen his claims covered in last year's New Age hit movie "What the
Bleep!?"
Many scientists view all this fuss about plain old H20 as standard
hippy-trippy nonsense with about as much credibility as crystal therapy.
Certainly Emoto's findings don't have much to do with the scientific method:
they are hand-picked, ad hoc and impossible to replicate. Yet though these
views are too far-out to take seriously, the findings of the latest bona
fide research are equally bizarre.
It now seems that the effects of water on living organisms transcend mere
chemistry: they are intimately linked to the most basic processes in the
cosmos. Put bluntly, you owe your existence to quantum effects in water that
make even the wackiest New Age ideas seem ho-hum.
If cornered, any scientist would have concede that water does have some odd
properties that are important for life. The fact that solid water-ice
-defies convention being less dense than its liquid state has stopped the
oceans from freezing solid from the bottom up and killing all marine life.
And the unusual reluctance of water to heat helped the oceans to iron out
climatic swings, giving organisms time to adapt.
The simple chemical formula of water belies the subtleties behind its
weirdness. The key to many of water's properties is not the chemical bonds
between the one oxygen atom and two hydrogen atoms that make up the
molecule. It is the links between hydrogen atoms in different molecules.
These hydrogen bonds are at least 10 times as weak as a typical chemical
bond, which means that while they can bind molecules together, they also
break easily at room temperature.
A single drop of water is therefore a seething melee of order and disorder,
with structures constantly forming and breaking up within it. The result is
a liquid with dozens of anomalous bulk properties, from a boiling point more
than 150°C higher than that of comparable liquids to a marked reluctance to
being compressed.
All the bonds affecting water molecules are ultimately caused by quantum
effects, but hydrogen bonds are the result of one of the strangest quantum
phenomena: so-called zero-point vibrations. A consequence of Heisenberg's
famous uncertainty principle, these constant vibrations are a product of the
impossibility of pinning down the total energy of a system with absolute
precision at any given moment in time. Even if the universe itself froze
over and its temperature plunged to absolute zero, zero-point vibrations
would still be going strong, propelled by energy from empty space.
Quantum lifeline
In the case of water, these vibrations stretch the bonds between hydrogen
atoms and their host oxygen atoms, enabling them to link up with
neighbouring molecules more easily. The result is the highly cohesive liquid
that keeps our planet alive.
Felix Franks of the University of Cambridge has a nice illustration of the
vital role this quantum effect plays. Just take some water and swap the
hydrogen for atoms of its heavier isotope deuterium. You end up with a
liquid that is chemically identical, yet poisonous to all but the most
primitive organisms. "The only difference is in the zero-point energy," says
Franks.
A growing number of researchers are now investigating the consequences of
this deep link between quantum effects and life. Recent advances in
theoretical methods, experimental techniques and brute computing power have
allowed them to study how water interacts with DNA, proteins and cells in
unprecedented detail.
The results are often unexpected, and challenge simplistic assumptions about
how life works. Certainly the fashionable view that the secret of life can
be summed up in a catalogue of genes and the proteins they code for looks
risibly simplistic. It is becoming clear that they cannot carry out even
their most basic functions without direct help from molecules of the
colourless, odourless curiosity that comes out of the tap. "Without water,
it is all just chemistry" says Franks, "but add water and you get biology."
Some of the most impressive evidence is emerging from studies of proteins.
Created from chains of amino acids linked up according to the instructions
of DNA, proteins are the workhorse molecules of life. They perform a host of
key functions, from fighting off invaders to catalysing reactions and
building fresh cells. Their precise action depends largely on their physical
shape, and water molecules have long been known to be vital in ensuring
amino acids curl up in the right way. Only now are researchers discovering
the mechanism.
What they are finding is an astonishingly delicate interplay of proteins and
water molecules, orchestrated by those all important hydrogen bonds. In
January, Florian Garczarek and Klaus Gerwert at the department of biophysics
at the Ruhr University of Bochum, Germany, reported on the role water
molecules play in a protein called bacteriorhodopsin, which is found in the
outer walls of primitive life forms (Nature, vol 439, p109).
Bacteriorhodopsin undergoes a simple form of photosynthesis, using light to
create a, source of chemical energy. Researchers have long suspected that
this process relies on the incoming light shifting protons around the
molecule, creating a charge difference that acts rather like a battery. An
obvious source of protons is the hydrogen nuclei of the water trapped within
the protein's structure, but no one had shown how this could work.
Enter Garczarek and Gerwert. They exposed bacteriorhodopsin to infrared
light, and found that the behaviour of the water molecules trapped within it
was far from that of idle captives. Once struck by photons of light, the
shape of the protein changed,
breaking some of the hydrogen bonds between the trapped water molecules. The
pair found that this triggered a chain of events in which fragments of some
water molecules and clusters of others interacted to move protons through
the protein.
This sophisticated process is all made possible by the quantum behaviour of
the hydrogen bonds in water. "Having bonds that can easily be formed but are
not too difficult to break is a big advantage," says Garczarek. The results
suggest that it is no accident that chains of amino acids trap water
molecules as they fold up to form a protein.
Hydrogen bonds are also turning out to have a profound role in the
functioning of that other key constituent of life, DNA. As with proteins,
new findings suggest it is time for a rethink of the familiar thumbnail
sketch of DNA as a double helix of four chemical bases.
To perform its biological functions, DNA has to carry out various
manoeuvres, twisting, turning and docking with proteins at just the right
place. No problem for a metre-long stringy molecule like DNA, one might
think. Yet on the far smaller scale where the real action takes place -
typically a few hundred bases - DNA is pretty rigid. And then there's the
mystery of how proteins meet up with just the right parts of the double
helix.
Biochemists have long suspected water molecules are important:
concentrations of them around DNA appear to correlate with biological
activity. It turns out that water undergoes radical changes as it approaches
the surface of DNA. As the molecules draw near the double helix, the
seething network of hydrogen bonds within bulk water becomes disrupted, and
the motion of individual molecules becomes more and more sluggish.
The latest research focuses on what happens around the "troughs" in the
double helix formed by specific base pairs. It seems that water molecules
linger longer and rotate more slowly around some base pairs than others.
Suddenly that link between hydration levels and biological activity doesn't
seem so perplexing. After all, the base pairs on DNA are the building blocks
of genes, and their sequence dictates the order in which amino acids are
stitched together to make proteins. If water molecules linger longer around
some base pairs than others, the level of hydration will mirror the sequence
of base pairs.
Monika Fuxreiter of the Hungarian Academy of Sciences Biological Research
Centre in Budapest believes that this explains how proteins and DNA
interact. She and her colleagues at BRC's Institute of Enzymology created a
computer simulation of DNA and a protein called BamHI, which uses water
molecules to cut DNA at very specific points.
They saw that adding virtual water molecules to the mix had a dramatic
effect. "The water molecules report the DNA sequence to the protein while it
is still some distance away," says Fuxreiter. "Then as the protein gets
closer, the water molecules are ejected from the site until it binds tightly
to the DNA."
According to Fuxreiter the water molecules relay messages to the protein via
electrostatic forces, which reflect the varying levels of hydration on the
DNA. They can even warn the approaching protein about potential problems
with the DNA before it arrives. If the DNA is distorted due to some defect
it becomes more hydrated and the protein can't make proper contact," says
Fuxreiter. "Instead, it moves to another site which is very good
biologically." Fuxreiter's team is now planning to test just how effective
water molecules are in determining where and when proteins bind to DNA.
That there is more to water than hydrogen and oxygen is something many
researchers welcome. But Rustum Roy, a materials scientist at Pennsylvania
State University in University Park goes further. He thinks it is time for a
radical overhaul of the scientific view of water - one which, he believes,
has been dominated by chemistry for too long. "It's absurd to say that
chemical composition dictates everything," he says. "Take carbon, for
example - the same atoms can give you graphite or diamond." In a review
paper published in Materials Research Innovations in December, Roy and a
team of collaborators called for a re-examination of the case against the
most controversial of all claims made for water: that it has a "memory".
The idea that water can retain some kind of imprint of compounds dissolved
in it has long been cited as a possible mechanism for homeopathy, which
claims to treat ailments using solutions of certain compounds. Some
homeopathic remedies are so dilute they
no longer contain a single molecule of the original compound - prompting
many scientists to dismiss homeopathic effects as imaginary. For how can
water with nothing in it act as anything other than water?
Roy believes this is too simplistic: "It is a naive, chemistry-schoolbook
argument." He argues that water has proved itself capable of effects that go
beyond simple chemistry, and these may imbue water with a memory. One way
this may occur, he says, is through an effect known as epitaxy: using the
atomic structure of one compound as a template to induce the same structure
in others.
Hidden depths
Epitaxy is routinely used in the microprocessor industry to create perfect
semiconductor crystals. And according to Roy, water already exhibits
epitaxial effects. "The 'seeding' of clouds is the growth of crystalline ice
on a substrate of silver iodide, which has the same crystal structure," he
says. "No chemical transfer whatsoever occurs."
Roy and his colleagues also point to another effect they believe has been
overlooked by mainstream scientists in their rush to dismiss homeopathy: the
vigorous shaking of the mixtures used, a process called succussion. The team
estimates that shock waves generated by the shaking can cause localised
pressures inside the water to reach over 10,000 atmospheres, which may
trigger fundamental changes in the properties of the water molecules.
Roy believes that by taking homeopathy seriously scientists may find out
more about water's fundamental properties. "The problem is that much more
research needs to be done to find the right techniques to probe the
properties of water reliably," he says.
However, many scientists question the very idea of taking homeopathy
seriously. The most recent review of the medical evidence found that
homeopathic remedies were no better than a placebo in all but a handful of
cases (Journal ofAlternative and Complementary Medicine, vol 11, p813). That
is likely to put the brakes on research into this aspect of water. "Rigorous
experiments need to be done to provide support for all scientific claims,"
says theoretical chemist David Clary at the University of Oxford. "I don't
think it is worth spending time on this." Chemist Martin Chaplin of London
South Bank University is more sympathetic: "I think there may be something
in it, but we need good experiments - and the best researchers won't go near
the subject."
The latest discoveries about the role of water in living processes may
change that, however. After decades of research, Franks sums up his view of
the simple little molecule we call H20 in terms that will put a smile on the
face of New Age hippies everywhere: "It's the magic ingredient that turns
lifeless powders on laboratory shelves into living things." *
Robert Matthews is visiting reader in science at Aston University,
Birmingham, UK. His latest book, "25 Big Ideas: The science that's changing
our world", is published by Oneworld
--
Dana Ullman, MPH
Homeopathic Educational Services
2124 Kittredge St.
Berkeley, CA. 94704
(510)649-0294
(800)359-9051 (orders only in the U.S.)
(510)649-1955 (fax)
dullman@igc.org OR dana@homeopathic.com
http://www.homeopathic.com
Below is a fabulous article on the STRUCTURE OF WATER and
HOMEOPATHY...and it is fascinating scientific verification of what those of
us involved in homeopathy may already know...
And one of the co-authors of this important new research is IRIS BELL,
MD, PHD...who is the head of research for Dr. Andrew Weil's Program in
Integrative Medicine at the University of Arizona. Iris is a HOMEOPATH, and
she has published some great research on homeopathy...she discussed her and
other important work at the NCH Conference a couple of weeks ago...and
H.E.S. (www.homeopathic.com) has just begun to sell the set of CD-audios for
the day-long workshop in which she spoke...she was BRILLIANT!
By the way...I just spoke at Stanford Medical School this week, and
there was a lot of interest in this subject when I mentioned this new work.
I'm giving two talks at UCSF's School of Medicine next week, and I cannot
wait to present this information to them. Basically, anyone who says that
there is nothing in "homeopathic water" are simply uninformed about the
nature of water (no surprise here!).
--Dana Ullman
New Scientist 8 April 2006
The Quantum Elixir
Water. It's the foundation of life on Earth. But what is it about H2O that
gives it this amazing ability, asks Robert Mathews
IN NEW AGE circles, everyone is talking about it: the magical properties of
the colourless, tasteless liquid the rest of us blithely refer to as water.
Between frequent gulps of the life-giving elixir, those initiated into its
secrets talk reverently of the work of Masaru Emoto, who is said to have
proved that water responds to the emotions of those around it. They describe
how Emoto has demonstrated that ice crystals made from water blessed by a
Zen monk look so much more beautiful than those exposed to messages of hate.
Many have bought his best-selling book detailing his findings, and many more
have seen his claims covered in last year's New Age hit movie "What the
Bleep!?"
Many scientists view all this fuss about plain old H20 as standard
hippy-trippy nonsense with about as much credibility as crystal therapy.
Certainly Emoto's findings don't have much to do with the scientific method:
they are hand-picked, ad hoc and impossible to replicate. Yet though these
views are too far-out to take seriously, the findings of the latest bona
fide research are equally bizarre.
It now seems that the effects of water on living organisms transcend mere
chemistry: they are intimately linked to the most basic processes in the
cosmos. Put bluntly, you owe your existence to quantum effects in water that
make even the wackiest New Age ideas seem ho-hum.
If cornered, any scientist would have concede that water does have some odd
properties that are important for life. The fact that solid water-ice
-defies convention being less dense than its liquid state has stopped the
oceans from freezing solid from the bottom up and killing all marine life.
And the unusual reluctance of water to heat helped the oceans to iron out
climatic swings, giving organisms time to adapt.
The simple chemical formula of water belies the subtleties behind its
weirdness. The key to many of water's properties is not the chemical bonds
between the one oxygen atom and two hydrogen atoms that make up the
molecule. It is the links between hydrogen atoms in different molecules.
These hydrogen bonds are at least 10 times as weak as a typical chemical
bond, which means that while they can bind molecules together, they also
break easily at room temperature.
A single drop of water is therefore a seething melee of order and disorder,
with structures constantly forming and breaking up within it. The result is
a liquid with dozens of anomalous bulk properties, from a boiling point more
than 150°C higher than that of comparable liquids to a marked reluctance to
being compressed.
All the bonds affecting water molecules are ultimately caused by quantum
effects, but hydrogen bonds are the result of one of the strangest quantum
phenomena: so-called zero-point vibrations. A consequence of Heisenberg's
famous uncertainty principle, these constant vibrations are a product of the
impossibility of pinning down the total energy of a system with absolute
precision at any given moment in time. Even if the universe itself froze
over and its temperature plunged to absolute zero, zero-point vibrations
would still be going strong, propelled by energy from empty space.
Quantum lifeline
In the case of water, these vibrations stretch the bonds between hydrogen
atoms and their host oxygen atoms, enabling them to link up with
neighbouring molecules more easily. The result is the highly cohesive liquid
that keeps our planet alive.
Felix Franks of the University of Cambridge has a nice illustration of the
vital role this quantum effect plays. Just take some water and swap the
hydrogen for atoms of its heavier isotope deuterium. You end up with a
liquid that is chemically identical, yet poisonous to all but the most
primitive organisms. "The only difference is in the zero-point energy," says
Franks.
A growing number of researchers are now investigating the consequences of
this deep link between quantum effects and life. Recent advances in
theoretical methods, experimental techniques and brute computing power have
allowed them to study how water interacts with DNA, proteins and cells in
unprecedented detail.
The results are often unexpected, and challenge simplistic assumptions about
how life works. Certainly the fashionable view that the secret of life can
be summed up in a catalogue of genes and the proteins they code for looks
risibly simplistic. It is becoming clear that they cannot carry out even
their most basic functions without direct help from molecules of the
colourless, odourless curiosity that comes out of the tap. "Without water,
it is all just chemistry" says Franks, "but add water and you get biology."
Some of the most impressive evidence is emerging from studies of proteins.
Created from chains of amino acids linked up according to the instructions
of DNA, proteins are the workhorse molecules of life. They perform a host of
key functions, from fighting off invaders to catalysing reactions and
building fresh cells. Their precise action depends largely on their physical
shape, and water molecules have long been known to be vital in ensuring
amino acids curl up in the right way. Only now are researchers discovering
the mechanism.
What they are finding is an astonishingly delicate interplay of proteins and
water molecules, orchestrated by those all important hydrogen bonds. In
January, Florian Garczarek and Klaus Gerwert at the department of biophysics
at the Ruhr University of Bochum, Germany, reported on the role water
molecules play in a protein called bacteriorhodopsin, which is found in the
outer walls of primitive life forms (Nature, vol 439, p109).
Bacteriorhodopsin undergoes a simple form of photosynthesis, using light to
create a, source of chemical energy. Researchers have long suspected that
this process relies on the incoming light shifting protons around the
molecule, creating a charge difference that acts rather like a battery. An
obvious source of protons is the hydrogen nuclei of the water trapped within
the protein's structure, but no one had shown how this could work.
Enter Garczarek and Gerwert. They exposed bacteriorhodopsin to infrared
light, and found that the behaviour of the water molecules trapped within it
was far from that of idle captives. Once struck by photons of light, the
shape of the protein changed,
breaking some of the hydrogen bonds between the trapped water molecules. The
pair found that this triggered a chain of events in which fragments of some
water molecules and clusters of others interacted to move protons through
the protein.
This sophisticated process is all made possible by the quantum behaviour of
the hydrogen bonds in water. "Having bonds that can easily be formed but are
not too difficult to break is a big advantage," says Garczarek. The results
suggest that it is no accident that chains of amino acids trap water
molecules as they fold up to form a protein.
Hydrogen bonds are also turning out to have a profound role in the
functioning of that other key constituent of life, DNA. As with proteins,
new findings suggest it is time for a rethink of the familiar thumbnail
sketch of DNA as a double helix of four chemical bases.
To perform its biological functions, DNA has to carry out various
manoeuvres, twisting, turning and docking with proteins at just the right
place. No problem for a metre-long stringy molecule like DNA, one might
think. Yet on the far smaller scale where the real action takes place -
typically a few hundred bases - DNA is pretty rigid. And then there's the
mystery of how proteins meet up with just the right parts of the double
helix.
Biochemists have long suspected water molecules are important:
concentrations of them around DNA appear to correlate with biological
activity. It turns out that water undergoes radical changes as it approaches
the surface of DNA. As the molecules draw near the double helix, the
seething network of hydrogen bonds within bulk water becomes disrupted, and
the motion of individual molecules becomes more and more sluggish.
The latest research focuses on what happens around the "troughs" in the
double helix formed by specific base pairs. It seems that water molecules
linger longer and rotate more slowly around some base pairs than others.
Suddenly that link between hydration levels and biological activity doesn't
seem so perplexing. After all, the base pairs on DNA are the building blocks
of genes, and their sequence dictates the order in which amino acids are
stitched together to make proteins. If water molecules linger longer around
some base pairs than others, the level of hydration will mirror the sequence
of base pairs.
Monika Fuxreiter of the Hungarian Academy of Sciences Biological Research
Centre in Budapest believes that this explains how proteins and DNA
interact. She and her colleagues at BRC's Institute of Enzymology created a
computer simulation of DNA and a protein called BamHI, which uses water
molecules to cut DNA at very specific points.
They saw that adding virtual water molecules to the mix had a dramatic
effect. "The water molecules report the DNA sequence to the protein while it
is still some distance away," says Fuxreiter. "Then as the protein gets
closer, the water molecules are ejected from the site until it binds tightly
to the DNA."
According to Fuxreiter the water molecules relay messages to the protein via
electrostatic forces, which reflect the varying levels of hydration on the
DNA. They can even warn the approaching protein about potential problems
with the DNA before it arrives. If the DNA is distorted due to some defect
it becomes more hydrated and the protein can't make proper contact," says
Fuxreiter. "Instead, it moves to another site which is very good
biologically." Fuxreiter's team is now planning to test just how effective
water molecules are in determining where and when proteins bind to DNA.
That there is more to water than hydrogen and oxygen is something many
researchers welcome. But Rustum Roy, a materials scientist at Pennsylvania
State University in University Park goes further. He thinks it is time for a
radical overhaul of the scientific view of water - one which, he believes,
has been dominated by chemistry for too long. "It's absurd to say that
chemical composition dictates everything," he says. "Take carbon, for
example - the same atoms can give you graphite or diamond." In a review
paper published in Materials Research Innovations in December, Roy and a
team of collaborators called for a re-examination of the case against the
most controversial of all claims made for water: that it has a "memory".
The idea that water can retain some kind of imprint of compounds dissolved
in it has long been cited as a possible mechanism for homeopathy, which
claims to treat ailments using solutions of certain compounds. Some
homeopathic remedies are so dilute they
no longer contain a single molecule of the original compound - prompting
many scientists to dismiss homeopathic effects as imaginary. For how can
water with nothing in it act as anything other than water?
Roy believes this is too simplistic: "It is a naive, chemistry-schoolbook
argument." He argues that water has proved itself capable of effects that go
beyond simple chemistry, and these may imbue water with a memory. One way
this may occur, he says, is through an effect known as epitaxy: using the
atomic structure of one compound as a template to induce the same structure
in others.
Hidden depths
Epitaxy is routinely used in the microprocessor industry to create perfect
semiconductor crystals. And according to Roy, water already exhibits
epitaxial effects. "The 'seeding' of clouds is the growth of crystalline ice
on a substrate of silver iodide, which has the same crystal structure," he
says. "No chemical transfer whatsoever occurs."
Roy and his colleagues also point to another effect they believe has been
overlooked by mainstream scientists in their rush to dismiss homeopathy: the
vigorous shaking of the mixtures used, a process called succussion. The team
estimates that shock waves generated by the shaking can cause localised
pressures inside the water to reach over 10,000 atmospheres, which may
trigger fundamental changes in the properties of the water molecules.
Roy believes that by taking homeopathy seriously scientists may find out
more about water's fundamental properties. "The problem is that much more
research needs to be done to find the right techniques to probe the
properties of water reliably," he says.
However, many scientists question the very idea of taking homeopathy
seriously. The most recent review of the medical evidence found that
homeopathic remedies were no better than a placebo in all but a handful of
cases (Journal ofAlternative and Complementary Medicine, vol 11, p813). That
is likely to put the brakes on research into this aspect of water. "Rigorous
experiments need to be done to provide support for all scientific claims,"
says theoretical chemist David Clary at the University of Oxford. "I don't
think it is worth spending time on this." Chemist Martin Chaplin of London
South Bank University is more sympathetic: "I think there may be something
in it, but we need good experiments - and the best researchers won't go near
the subject."
The latest discoveries about the role of water in living processes may
change that, however. After decades of research, Franks sums up his view of
the simple little molecule we call H20 in terms that will put a smile on the
face of New Age hippies everywhere: "It's the magic ingredient that turns
lifeless powders on laboratory shelves into living things." *
Robert Matthews is visiting reader in science at Aston University,
Birmingham, UK. His latest book, "25 Big Ideas: The science that's changing
our world", is published by Oneworld
--
Dana Ullman, MPH
Homeopathic Educational Services
2124 Kittredge St.
Berkeley, CA. 94704
(510)649-0294
(800)359-9051 (orders only in the U.S.)
(510)649-1955 (fax)
dullman@igc.org OR dana@homeopathic.com
http://www.homeopathic.com