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For alternative meanings see proton (disambiguation).

Proton

Classification

Subatomic particle Fermion Hadron Baryon Nucleon Proton

Properties

Mass: 1.672 621 71(29) × 10−27 kg   938.272 029(80) MeV/c2 Electric Charge: 1.602 176 53(14) × 10−19 C Diameter: about 1.5×10−15 m Spin: ½ Quark Composition: 1 down, 2 up

In physics, the proton (Greek proton = first) is a subatomic particle with an electric charge of one positive fundamental unit (1.602 × 10⁻¹⁹ coulomb), a diameter of about 1.5×10⁻¹⁵ m, and a mass of 938.3 MeV/c² (1.6726 × 10⁻²⁷ kg), or about 1836 times the mass of an electron. The proton is observed to be stable, with a lower limit on its half-life of about 10³⁵ years, although some theories predict that the proton may decay. The proton has a density of about 2.31 × 10¹⁷ kg m⁻³.

Protons are spin-1/2 fermions and are composed of three quarks, making them baryons. The two up quarks and one down quark of the proton are also held together by the strong nuclear force, mediated by gluons. Protons may be transmuted into neutrons by inverse beta decay (that is, by capturing an electron); since neutrons are heavier than protons, this process does not occur spontaneously but only when energy is supplied. The proton's antimatter equivalent is the antiproton, which has the same magnitude charge as the proton but the opposite sign.

Protons and neutrons are both nucleons, which may be bound by the nuclear force into atomic nuclei. The most common isotope of the hydrogen atom is a single proton. The nuclei of other atoms are composed of various numbers of protons and neutrons. The number of protons in the nucleus determines the chemical properties of the atom and which chemical element it is.

In chemistry and biochemistry, the proton is thought of as the hydrogen ion, denoted H⁺. In this context, a proton donor is an acid and a proton acceptor a base (see acid-base reaction theories).

Proton Donor:

The donor of a proton in an acid-base reaction; that is, a Bronsted-Lowry acid

pH

pH is a measure of effective concentration of hydrogen ions in a solution. It is approximately related to the molarity of H⁺ by pH = - log [H⁺]

ORP stands for Oxidation-Reduction Potential. In practical terms, it is a measurement to oxidize contaminants.  ORP is the only practical method we have to electronically monitor sanitizer effectiveness. When chemists first used the term in the late 18th Century, the word "oxidation" meant, "to combine with oxygen."

We now know that oxidation involves an exchange of electrons between two atoms. The atom that loses an electron in the process is said to be "oxidized." The one that gains an electron is said to be "reduced." In picking up that extra electron, it loses the electrical energy that makes it "hungry" for more electrons.

We also know that matter can be changed, but not destroyed. You can alter its structure, and can increase or decrease the amount of energy it contains - but you can't eliminate the basic building blocks that make things what they are.

Chemicals like chlorine, bromine, and ozone are all oxidizers. It is their ability to oxidize - to "steal" electrons from other substances - that makes them good water sanitizers, because in altering the chemical makeup of unwanted plants and animals, they kill them. Then they "burn up" the remains, leaving a few harmless chemicals as the by-product.

Of course, in the process of oxidizing, all of these oxidizers are reduced - so they lose their ability to further oxidize things. They may combine with other substances in the water, or their electrical charge may simply be "used up." To make sure that the chemical process continues to the very end, you must have a high enough concentration of oxidizer in the water to do the whole job.

But how much is "enough?" That's where the term potential comes into play.

"Potential" is a word that refers to ability rather than action. We hear it all the time in sports. ("That rookie has a lot of potential - he hasn't done anything yet, but we know that he has the ability to produce.)

Potential energy is energy that is stored and ready to be put to work. It's not actually working, but we know that the energy is there if and when we need it. Another word for potential might be pressure. Blow up a balloon, and there is air pressure inside. As long as we keep the end tightly closed, the pressure remains as potential energy. Release the end, and the air inside rushes out, changing from potential (possible) energy to kinetic (in motion) energy.

In electrical terms, potential energy is measured in volts. Actual energy (current flow) is measured in amps. When you put a voltmeter across the leads of a battery, the reading you get is the difference in electrical pressure - the potential - between the two poles. This pressure represents the excess electrons present at one pole of the battery (caused, incidentally, by a chemical reaction within the battery) ready to flow to the opposite pole.

When we use the term potential in describing ORP, we are actually talking about electrical potential or voltage. We are reading the very tiny voltage generated when a metal is placed in water in the presence of oxidizing and reducing agents. These voltages give us an indication of the ability of the oxidizers in the water to keep it free from contaminants.

If we had a body of water in which the concentration of oxidizers (or oxidants as chemists are apt to say) exactly equaled the concentration of reducers (reductants), then the amount of potential generated at the measuring electrode would be exactly zero. As you might guess, the water would be in pretty sad shape, because if any additional contaminants were introduced into the water, there would be no oxidizer to handle it.

As we add oxidizer to the water, it "steals" electrons from the surface of the platinum measuring electrode. To make things a little more confusing, we need to point out that electrons are negatively charged particles. When we remove these negatively charged things from this electrode, the electrode becomes more and more positively charged. As we continue to add oxidizer to the water, the electrode generates a higher and higher positive voltage.

In 1972, the World Health Organization adopted an ORP standard for drinking water disinfection of 650 millivolts. That is, the WHO stated that when the oxidation-reduction potential in a body of water measures 650/1000 (about 2/3) of a volt, the sanitizer in the water is active enough to destroy harmful organisms almost instantaneously.

In Germany, which has about the strictest water quality standards in the world, an ORP level of 750 millivolts has been established as the minimum standard for public pools (1982) and spas (1984).

ORP devices can be used to measure sanitizer effectiveness and to control ozone generators.

Understanding pH and ORP measurements

ORP stands for Oxidation – Reduction Potential

It measures the potential for a liquid solution to be an Oxidizer or a Reducer.

Oxidizers – Accept electrons or strip electrons from another compound.  This is what free radicals do in the body. They strip electrons from the cell membrane walls or from the DNA of the nucleus and damage the cell. Free radicals are opposed or neutralized by anti-oxidants. The mitochondria of the cells, where energy is produced, generate free radicals in the form of highly charged oxygen (singlet oxygen, O2- and OH-) and metabolic waste.  Very powerful anti-oxidants, like Coenzyme Q10, Alpha-Lipoic Acid and Lycopene surround the mitochondria to prevent the escape of the free radicals.

The metabolic waste is generally a weak acid, ie lactic acid.  Liquid solutions with a positive ORP are oxidizers and have an acidic pH.  Water with dissolved oxygen will have a positive ORP and be a weak oxidizer.  Iron will rust in well water, but bacteria will grow.  Ozone and Chlorine are strong oxidizers and are powerful disinfectants when added to water.  The ORP will be very high and bacteria die.  ORP is used in many industries to measure water quality.  A water with a high ORP will also be a low pH or acidic water.  Acid solutions are proton donors (H+).  A solution of HCL, hydrochloric acid, is an ionic mixture of H+ and CL-.  The pH will be very low, acidic, depending on the concentration of the HCL added to the water and the ORP will be high.  Stomach acid for example is used to destroy incoming bacteria.  It is a strong oxidizer and disinfectant.  It also starts the breakdown of proteins.  ORP and pH are used together to control many chemical reactions

Reducers – Donate electrons or give up electrons to other compounds.  Anti-oxidants give up electrons to the free radicals to neutralize them.  A liquid solution that has a negative ORP will be a reducer. It will give up electrons.  Anti-oxidants are unique in that they can give up an electron without becoming a free radical in search of an electron.  Negative ORP readings are also associated with a high pH value or alkaline.  They can donate electrons or accept protons.  By accepting protons alkaline solutions neutralize acids.  Pure water is a neutral pH of 7 and a 0 ORP.  Additives move both the ORP and the pH.  Certain minerals can raise the ORP and other minerals lower the ORP.  Tap water can be through an ionizer to create two separate streams.  One stream will have a positive ORP and low pH in response to the acidic minerals it contains and the other will have a negative ORP and high pH and be called alkaline water. The degree of separation depends on the quality of the machine.  Alkaline water is thought to be healthy to drink to help neutralize the acidic waste being generated in the body.  The acidic water is thought to be good to wash your hands with because of its antiseptic properties.  It is also recommended to water your plants with the acid water to improve soil conditions. Hence there is a thought that the alkaline water with its high pH and low ORP is the standard for judging healthy water.  That is a mistake.

An alkaline water used long term is going to slowly neutralize the stomach acid and change the pH of the intestinal tract.  This will lead to long term problems with protein and fat metabolism.  Both are highly pH dependent.  There will also be a slow accumulation of pathogenic bacteria in the gut which can produce ulcers and inflammation of the gut, such as Chron’s disease.  The upper part of the GI tract is designed to operate at a fairly acidic pH of 5.6.  A high pH water may be good for someone who is highly toxic and producing a large amount of metabolic waste. But it is a short term solution.  Also the alkaline waters have not been demonstrated to be hydrating to the cells.  They may add some minerals to buffer the blood pH, but that does not mean the water tranverses through the aquaporin channels to hydrate the cells.

What you really want to do is eliminate the production of the metabolic waste.  Since metabolic waste is generated in the Krebs cycle of the mitochondria, it is critically important to realize how the body produces energy through the conversion of ADP to ATP.  This is described in the paper Applied BioLogics found on The Stowe Foundation website, www.thestowefoundation.org. The mitochondria are the organelles contained within each cell of the body that produce energy. The mitochondria use the enzymes of the Krebs cycle to convert blood glucose into energy.  These enzymes must be contained in cellular water to operate efficiently.  The interior of the mitochondria is the deepest spot that water must penetrate.  Any water that can not deliver superior cellular hydration will not affect the hydration of the mitochondria.  Dehydrated mitochondria will short circuit the electron transfer capacity of the mitochondrial enzymes. Energy production is inefficient and the cells generate lots of metabolic waste.

In other activities, such as intense exercise, oxygen to the muscles is in short supply and the muscles will begin to use anerobic pathways to keep producing energy for as long as possible.  These enzymes require proton donors and the body will produce lactic acid as the source of protons.  When the exercise ceases the lactic acid must be swept from the cells, which also requires cellular hydration.  The key and most fundamental property of water is very simple.  Does it hydrate the cells or not?  HYDRATE8X has proven to have the right structure and physical properties to hydrate the cells. It also has the correct ORP and pH to support and not degrade the intestinal tract.  That is why you never get the intestinal bloating when you drink HYDRATE8X.  Also HYDRATE8X can serve as a proton donor deep within the mitochondria to keep energy production efficient and hence limit the production of metabolic free radicals. Hydration is the key and the ability of being a proton donor is a very special feature.

The ORP measurements of HYDRATE8X show that our ozone process has disinfected the water and dissolved extra oxygen into the water.  It also shows that HYDRATE8X can be a proton donor.  By hydrating the cells all the way to the level of the mitochondria with a proton donating water, HYDRATE8X has established a new category of water.  It should not be compared to alkaline water that has limited benefits to the body.  Anti-oxidant waters limit the damage of energy production, but HYDRATE8X improves the efficiency of energy production and therefore allows the body’s normal anti-oxidant systems to be sufficient.   In fact, our sports energy drink will enhance the proton donor capacity of the water and will write a new chapter in sports physiology.

How The Mitochondria Work

Condensed from the internet

The chemiosmotic theory (def) explains the functioning of electron transport chains. According to this theory, the transfer of electrons down an electron transport system through a series of oxidation-reduction reactions (def) releases energy (see Fig. 1). This energy allows certain carriers in the chain to transport hydrogen ions (H⁺ or protons) across a membrane.

Depending on the type of cell, the electron transport chain may be found in the cytoplasmic membrane or the inner membrane of mitochondria.

• In prokaryotic cells, the protons are transported from the cytoplasm of the bacterium across the cytoplasmic membrane to the periplasmic space located between the cytoplasmic membrane and the cell wall .
• In eukaryotic cells, protons are transported from the matrix of the mitochondria across the inner mitochondrial membrane to the intermembrane space located between the inner and outer mitochondrial membranes (see Fig. 4).

As the hydrogen ions accumulate on one side of a membrane, the concentration of hydrogen ions creates an electrochemical gradient or potential difference (voltage) across the membrane. (The fluid on the side of the membrane where the protons accumulate acquires a positive charge; the fluid on the opposite side of the membrane is left with a negative charge.) The energized state of the membrane as a result of this charge separation is called proton motive force (def) or PMF.

This proton motive force provides the energy necessary for enzymes called ATP synthases (see Fig. 5), also located in the membranes mentioned above, to catalyze the synthesis of ATP from ADP and phosphate. This generation of ATP occurs as the protons cross the membrane through the ATP synthase complexes and re-enter either the bacterial cytoplasm (see Fig. 2) or the matrix of the mitochondria. As the protons move down the concentration gradient through the ATP synthase, the energy released causes the rotor and rod of the ATP synthase to rotate. The mechanical energy from this rotation is converted into chemical energy as phosphate is added to ADP from ATP.

Proton motive force is also used to transport substances across membranes during active transport and to rotate bacterial flagella.

At the end of the electron transport chain involved in aerobic respiration, the last electron carrier in the membrane transfers 2 electrons to half an oxygen molecule (an oxygen atom) that simultaneously combines with 2 protons from the surrounding medium to produce water as an end product (see Fig. 3).

The cell energy production circuit is known as the Krebs cycle and is located inside the mitochondria of each cell.  A mitochondrion is the organelle that produces energy for the cell and each cell has multiple energy production centers.  It is the energy production cycle that produces free radicals such as singlet oxygen that can damage the cell.  In order to prevent cell damage, the mitochondria are surrounded with anti-oxidants and specific enzymes, such as super oxide dismutase (SOD) and glutathione, to neutralize and control damaging free radicals.  Our life force is maintained by the production of energy, so we are always producing free radicals.  Therefore, it is critical that we maintain a high degree of quality control over the energy production cycle.  The body breaks down without proper maintenance on the engine.

Peter Mitchell, a British chemist, won the 1978 Nobel Prize for chemistry for helping to clarify how ADP (adenosine diphosphate) is converted into the energy carrying compound ATP (adenosine triphosphate) in the mitochondria of living cells.  ATP is made within the mitochondria by adding a phosphate group to ADP in a process known as oxidative phosphorylation.  Mitchell was able to determine how the different enzymes involved in the conversion of ADP to ATP are distributed within the membranes that partition the interior of the mitochondrion.  He showed how these enzymes arrangement facilitates their use of hydrogen ions (protons, H+) as an energy source in the conversion of ADP to ATP.  Later scientists have described this phenomenon as the proton motive force and the proton wave effect.  The Krebs cycle requires a source of protons (H+) from proton donors.

The most common proton donor studied in the Krebs cycle, also referred to as the citric acid cycle, is nicotinamide adenine dinucleotide (NADH).  NADH is a coenzyme made from vitamin B2 or niacin.  It is present in all living cells.  As a coenzyme, NADH serves to make the enzymes of the Krebs cycle work.  The Krebs cycle is often described more in terms of an electron transport mechanism in which enzymes catalyze sequential oxidation reduction reactions.  The fuel for the Krebs cycle is blood glucose and the agent for oxidation is oxygen.  However, hydrogen protons (H+) are required for the reduction reactions.  Therefore, the electron transport required to generate energy can only occur when the sequential oxidation reduction reactions are coupled together.  The coupling mechanism is provided by the proton flux and this requires the presence of proton donors.

Very advanced work by Markus Meuwly and published in the Faraday Discussions suggests that the diffusion of water (H2O) into the active site of an electron coupled proton transfer is an attractive alternative to direct proton transfer from the protein matrix of ferredoxins.  The ferredoxins are proteins that contain one or more iron-sulphur clusters, which makes such proteins eminent in electron transfer reactions.  Ferredoxins are a major component of the Krebs cycle.  Meuwly’s work suggests that the water molecule could serve as a possible proton donor.

Meuwly’s work demonstrates why chronic illness is always associated with dehydration at the cellular level.  The mitochondria are being deprived of a source of proton donors, cellular H2O, which is also biomolecular water or structured water.  The water in our cells is an active participant in the chemical reactions that occur in our mitochondria.  The mitochondria are the original hydrogen fuel cell.

The body uses a complex system of catalysts (enzymes and coenzymes) within the mitochondria to achieve energy efficiency.  A catalyst is a compound that can lower the activation energy of a given chemical reaction.  In the human body, catalysts are known as enzymes and the coenzymes that make the enzymes work.  We know that many coenzymes are derived from the B-vitamins and hence diet plays critical role in health.

A second major factor in the proper function of the enzymes are the metals (trace minerals in nutritional terms) attached to the amino acid sequences that form the basic protein structure of the enzyme.  It is the trace minerals that easily transfer electrons from one compound to another.  This is the heart and sole of energy production, the transfer of electrons.  A fundamental concept in the attachment of a trace mineral or metal to a protein structure is the binding energy of the metal.  How easily does the metal or trace mineral attach to the enzyme?  Basically, metals are competitive with each other.  This has major implications in health.

It is straight forward science that a metal, like cadmium, found in the paper of cigarettes and inhaled with every puff or breathed in through second hand smoke, can displace the biologically active metals of zinc, selenium and magnesium (the trace minerals) from the biologically active enzymes.  Cadmium has a stronger binding coefficient for the amino acid structure of the enzyme than the trace minerals.  When cadmium or mercury or any other heavy metal displaces a trace mineral like zinc or selenium from the enzyme it does not function properly as a catalyst.  Electrons flow undirected through the cellular matrix and free radical pathology can spin out of control.  You can not take enough anti-oxidants to keep up with the free radical production and hence inflammation becomes a permanent part of your life.   The energy balance of the body is disrupted.  In the oil refining industry they would say the catalyst has become contaminated or poisoned.  In that event, the refinery catalyst is replaced with a fresh batch.  This is not so easily accomplished in the body.

In the human body, the proper energy balance can only be restored by decontaminating or detoxifying the body.  That is, remove the catalytic poisons (like cadmium, lead, mercury, arsenic, aluminum, nickel) that are attached to the enzymes and replenish them with the proper energetic metals like selenium and zinc.  This is the essence of chelation therapy and trace mineral replacement.  Remove the toxic heavy metals and restore the beneficial trace minerals.  Then the mitochondria can function and our life force restored.  Through the concepts of Applied BioLogics, we understand the importance and the science of energy medicine. Making sure the body operates at the right energy levels is pure science and engineering.  When enzymes start to fail on a systemic basis, then it is time to look at enzyme therapy, with enzyme supplements to compensate for the dysfunctional pathways.  It is also time to look at how to detoxify the body.  The body will only be restored to true health when the enzyme poisons have been removed and proper controls put on free radical pathology.

In fact, there are encouraging signs that the concepts of energy medicine are starting to permeate the medical field.  Work performed at the Mayo Clinic by Dzeja and Terzic states; “at the level of the mitochondria and the nucleus of the cell, precise coupling of spatially separated intracellular ATP-producing and ATP-consuming processes is fundamental to the bioenergetics of living organisms, ensuring a fail-safe operation of the energetic system over a broad range of cellular functional activities.  Mechanisms responsible for communication between spatially separated intracellular ATP consumption and ATP production processes, and their precise coupling over a broad range of cellular functional activity has remained a long-standing enigma.  Distribution of cellular energy could be accomplished by altering phosphotransfer enzyme isoform composition and their intracellular localization.  In this regard, derangement in cellular energy flow and distribution has been implicated in cardiovascular and neurodegenerative diseases, as well as in determining uncontrolled growth and metastatic potential of tumor cells”.

The cliff note version of these statements is that enzymes contained in the mitochondria, the cytoplasm and the nucleus of the cell are responsible for the energy production, the energy transfer and the energy utilization within the cell.  The enzymes must be located a proper distance from each other in order to achieve a balanced flow of energy.  When energy flow is disturbed then cells do not function properly and major problems show up, such as heart disease, diabetes, dementia and cancer.

Functional medicine must look at the energy status of the body and this requires a very close examination of the enzymatic pathways of the body.  The primary determinant of the spatial alignment of enzymes is cell hydration.  Cellular water determines cell volume and whether the cell is swollen or dehydrated.  Too much water and the enzymes will be too far apart.  Too little cellular hydration and the enzymes will interfere with each other.  Cellular hydration plays two critical roles in cell health, the spatial separation of the enzymes and the potential to be a proton donor.

Enzymes that are contaminated with toxins are not going to work.  Make no mistake, America is loaded with toxins.  The heavy metal toxins are quite prevalent.  Mercury is found in the fish we eat and the silver fillings we put in our mouth, cadmium is found in cigarette smoke, arsenic throughout many of the water supplies due to industrial pollution and lead from paints and fuels.  Aluminum and nickel are being monitored as contributing factors to Alzheimers and Parkinson’s disease.  We even use barium in medical diagnostic tests.  Exposure to heavy metals is easy to come by and the heavy metals have an affinity to attach themselves to the enzymes.  The body will accumulate a toxic load over time.  It shows up in our bodies as accelerated aging and chronic illness. Tissue samples taken from breast cancer patients often show 30,000 times the level of mercury as thought safe.

The FDA and EPA recently released warnings to pregnant mothers to avoid mercury contaminated fish, which included tuna and swordfish.  The reason given was to avoid damage to the developing fetus, in particular, to avoid fetal brain damage.  The mother should be well advised that mercury is not selective to the fetus.  It will harm her as well as the fetus.

Mercury is even used in laboratory experiments as the toxin most easily applied to disrupt the flow of water into human cells through the aquaporin channels.  The aquaporin channels are essentially enzymatic pathways that transport water into and out of the cells and cellular water into and out of the organelles of the cells like the mitochondria.

The aquaporin channels depend on the proper electrical charge on the enzymes to function.  Mercury or any heavy metal can easily disrupt the electrical field of the aquaporin channel.  Dehydration at the cellular level is common among all chronic illness.  This can easily be the result of toxins shutting off the aquaporin channels.  Clinical studies show that hydration affects human performance at every level of the body.  Toxins interfere with hydration and the enzymatic performance in the cells, the mitochondria and the cell membrane walls.  Heavy metals are very nasty enzyme poisons and must be considered a cofactor in every chronic illness.  But heavy metals are not the only toxins that can affect enzyme performance.

Most of the chemical toxins we are exposed to in our daily lives, such as herbicides, insecticides and pesticides are chlorine or fluorine based.  Agent Orange is probably the best known herbicide and it is extremely toxic to the human body.  Fluorine and chlorine are chemically known as halogens and are extremely reactive substances.  We are advised not to swallow our fluoridated toothpaste and to not use it with infants.  Exposure to halogens also comes from flame retardant chemicals found on our carpets and upholstery plus baby clothes and cribs.  These toxins can also disable enzymatic activity and membrane permeability which leads to uncontrolled free radical pathology and the accumulation of metabolic waste.  Toxins are the silent killers.

Electron Coupled Proton Transfer in Ferredoxins

Ferredoxins are proteins that contain one or several iron-sulphur clusters. This makes such proteins eminent in electron transfer reactions. FdI is a particularly intensely investigated iron-sulphur protein for which also mutants have been crysallized and spectroscopically characterized. This allows to compare theoretical investigations with a variety of experimental data and validate the approach taken.

Because Fd I (PDB code 7FDR) contains a [3Fe-4S] and a [4Fe-4S] cluster, first parameters for describing the electrostatics and the bond-, angle-, and dihedral-terms in the molecular dynamics force field have to be derived. This is done using ab initio calculations. Density functional theory has shown to be very suitable for such investigations. We used UB3LYP with the 6-31G** basis set to calculate optimized structures of the isolated [3Fe-4S]^(0/+) and the biologically more relevant [3Fe-4S]^(0/+)(SCH₃)₃ cluster which is closer to the situation in the protein. Charges are calculated using standard Mulliken, the ESP and NBO method. All three charge sets are used in the molecular dynamics calculations.

Analysis of the experimental results suggested that the protonation occurs directly from the protein matrix to the FeS cluster. However, in our MD simulations, we observed a number of other candidate-hydrogen atoms that could possibly serve as proton donors. In particular, the suggested proton at Asp15 is generally too far away from the FeS cluster to serve as an ideal candidate. The other protons from surrounding side chains are usually strongly bound. A possible reaction mechanism involves the additional protonation of the protein side chain from solvent water which would make the NH of Asp15 less acidic. However, an attractive alternative to direct proton transfer from the protein matrix is the diffusion of water into the active site. We have shown that such a water molecule is dynamically stable and indeed could serve as a possible proton donor.[1] Also, differences between a fast (native protein) and slow (D15E mutant) variant of the protein were observed in the MD simulations that could account for the observed slowdown of an order or magnitude upon mutating Asp15-->Glu15.[2,3]

[1] M. Meuwly and M. Karplus, Farad. Disc. Royal. Soc. 124, 297 (2003)
[2] K. Chen, J. Hirst, R. Camba, C. A. Bonagura, C. D. Stout, B. K. Burgess and F. A. Armstrong, Nature, 405, 814-817 (2000)
[3] M. Meuwly and M. Karplus, Biophys. J., in print (2004)

Uses of nuclear magnetic resonance

The most obvious use of nuclear magnetic resonance is in magnetic resonance imaging for medical diagnosis, however, it is also widely used in chemical studies, notably in NMR spectroscopy such as proton NMR and carbon-13 NMR.

These studies are possible because nuclei are surrounded by orbiting electrons, which are also spinning charged particles such as magnets and, so, will partially shield the nuclei. The amount of shielding depends on the exact local environment. For example, a hydrogen bonded to an oxygen will be shielded differently than a hydrogen bonded to a carbon atom. In addition, two hydrogen nuclei can interact via a process known as spin-spin coupling, if they are on the same molecule, which will split the lines of the spectra in a recognisable way.

By studying the peaks of nuclear magnetic resonance spectra, skilled chemists can determine the structure of many compounds. It can be a very selective technique, distinguishing among many atoms within a molecule or collection of molecules of the same type but which differ only in terms of their local chemical environment.

By studying T₂* information a chemist can determine the identity of a compound by comparing the observed nuclear precession frequencies to known frequencies. Further structural data can be elucidated by observing spin-spin coupling, a process by which the precession frequency of a nucleus can be influenced by the magnetization transfer from nearby nuclei.

T₂ information can give information about dynamics and molecular motion.

The dynamics and molecular motion of the hydrogen proton can be directly correlated to the physical properties of the molecule.