Sooner or later, those who think extensively and effectively about the advance of science and technology and about the preservation of freedom and free enterprise, which are essential to that advance, become concerned with the problem of education - both that of scientists and technologists and also that of the citizenry in general. They realize that it is not possible for these disciplines to flourish very long in a civilization in which most of the individual citizens are unable or unwilling to learn and to think.

The majority of those who control American primary and university education and American corporate and political power do not, of course, agree with this premise. Theirs is essentially an elitist view wherein a top stratum of society monopolizes knowledge, wealth, and power, while the "masses'' beneath must be taught proper behavior rather than independent thought. This is not surprising. Human history is, to a large extent, a sorry, several thousand year record of one elite after another trying to run the world and ultimately failing -with general suffering for everyone in the course of each such failure.

There is, however, enormous strength in the Constitutionally protected free republic (not democracy) that was bequeathed to America by our founding fathers. Regardless of the depredations of two centuries of elitist assaults on that freedom, 250 million Americans, continuously revitalized by immigration of freedom-loving people from many other lands, have great vitality and productive potential.

It is the nature of a free society that, when an important aspect of civil life begins to fail, new approaches arise spontaneously to replace the failures. If the failure has been an especially important one, then the changes can appear to be revolutionary in scope. Any amount of positive change at any sustainable rate is acceptable, providing the freedom itself that makes change possible is not undermined.

At present, this sort of revolution is underway in American education. The institutions that have provided education in America have gradually succumbed to the underlying flaw that they are based upon socialism. At every level - academic, social, and spiritual - American primary and secondary schools and American colleges and universities are failing and are being perceived as failures by an increasingly large percentage of the American people. Moreover, this is occurring at the same time that the revolution in computer technology is shattering the monopoly that educational institutions have held on information as a result of the previously high cost of maintaining great libraries and other storehouses of knowledge.

The most obvious symptom of this collapse is the very rapid rise of home schooling. From a relatively rare curiosity, home schooling has risen so rapidly during the past ten years that estimates of more than one million American children currently being educated by their families entirely outside of educational institutions are realistic.

We have recently sampled the intensity of this movement. In April, we mailed a two-page advertisement and a six-page article about home schooling to a mailing list that a previous test had indicated would be a good market for our home school CDs. The mailing was successful and a small profit was realized, which will help with production of more CDs. Astonishing, however, were the letters and telephone calls - more than 1,000 so far and still arriving here at a rate that exceeds our ability to respond to them. As I have talked with these people (mostly Americans who are determined to obtain quality education for their children), I have come to realize that I am becoming an advocate of certain simple truths that have apparently been lost to many people. These are that:

Consider one example drawn from education in math and science - the very important skill and foundation of independent thought, problem solving - especially the so-called "word problem'' in which the student must conceptualize the problem and reduce it to a form for which mathematics enables a solution. This ability is acquired by solving problems - tens of thousands of them, starting with the level of a six-year-old child and extending gradually to university level physics and chemistry and beyond.

The outlook for American science and technology is, however, very bright - because of American freedom. If present trends continue and free enterprise has its way, American tax-supported schools will collapse and disappear (including a large percentage of colleges and universities) and will be replaced by free-market alternatives that are already growing very rapidly. I think that this will happen within the lifetimes of many current readers of Access to Energy.

At the DDP meeting last year in Grants Pass, Oregon, Professor R. B. Merrifield described several projects proceeding in his and other laboratories using solid phase synthesis - the methodology that he invented and used for the first laboratory synthesis of an enzyme and for which he received the Nobel Prize in Chemistry. (Audio tapes are still available from DDP at telephone (520) 325-2680.)

One of the current projects that he described is the synthesis of a new class of antibiotics modeled on peptide sequences found in silk moths and honey bees. The 26 residue peptide that Dr. Merrifield and his coworkers have made is active against gram-negative and gram-positive bacteria. Moreover, synthesis of this peptide with "d'' isomer amino acid residues enhances its activity and protects the peptide from degradation by ordinary enzymes (since these preferentially degrade peptides with "1" isomer amino acid residues). The "d" form of the peptide is several times more active against bacteria than are ordinary antibiotics currently in widespread use.

This discovery is especially important because of the recent rapid rise of strains of disease-causing (such as tuberculosis) bacteria that are immune to antibiotics. Peptide antibiotics are expected to be effective against these new strains. Also, peptide antibiotics are easily modified by changes in amino acid residue sequence, so future new bacterial strains can probably be countered by changes in sequence.

At present, it is questionable whether or not this antibiotic will ever be made available to the American public because regulatory costs im- posed on new drugs by government bureaucrats involve years of de- lays and expenditures of more than $100 million per drug. Therefore, in addition to business risks and the cost of engineering, mass produc- tion facilities, marketing, and other things, ridiculous amounts of time and money must be spent appeasing bureaucrats.

Professor Merrifield founded an entire branch of synthetic organic chemistry - solid phase synthesis. Solid phase synthesis has already had a very profound effect upon chemistry, biochemistry, molecular biology, and medical science, and that effect is expanding rapidly as a result of new techniques that have been derived from solid phase syn- thesis. The most recent is being called "combinatorial chemistry," as described by R. E. Service in "Combinatorial Chemistry Hits the Drug Market," Science 272, pp 1266- 1268 (1996). Combinatorial chemistry allows a chemist to make thousands or sometimes millions of differ- ent compounds simultaneously and test each compound for optimum utility in solving a particular problem of interest.

How this is done can be explained by reference to the original development by Merrifield of solid phase synthesis:

The most important molecules in living things are those called "peptides." Large peptides are called "proteins" or, if they are known to catalyze (accelerate) particular chemical reactions, "enzymes." Other types of peptides have special names. Some are "hormones," some are "structural proteins" (comprising cell walls or membranes), and some have other functions. Snake venoms, for example, are peptides. All peptides (with rare exceptions) are simply long chains constructed from 20 different amino acids. (Actually, two of the 20 are imino acids, but are not usually so designated.) These same 20 amino acids are used for all peptides, but the order in which they appear in the chain and the length of the chain varies in accordance with the required structure and function of each molecule. Each amino acid has two couplers that enable it to be incorporated into peptide chains - an amino group on one end and a carboxyl group on the other.

These can be caused to react to form a "peptide bond," which joins two amino acids together. The two can then react with an- other amino acid to form a tripeptide (three amino acid peptide) and so on to any desired length. The 20 amino acids differ in that each has an individual side chain group that confers unique chemical properties on the position in the peptide chain occupied by that amino acid. Some of these side chains are negatively charged, some positively charged, some acidic, some basic, some long, some short, most stable, some unstable, and each unique. A set of 20 has been selected so that, from these building blocks, virtually any desired shape, size, and chemically functional peptide can be created for any biochemical purpose. If it has the knowledge of the sequence of amino acids required, a living thing can make any peptide it needs to carry out any chemical function it desires.

DNA (deoxyribonucleic acid) is simply a library that remembers peptide sequences and communicates them efficiently to the peptide making machinery in a living thing. Since DNA is made of chains of only four different chemical groups, it requires a three-letter code to represent each of the 20 amino acids.

An amino acid can have either of two structures differing in that they are mirror images of one another. (With your copy of Access to Energy in one hand, stand looking in a mirror, and then mentally remove your image from the mirror and try to superimpose it on yourself.  The fact that you cannot shows that the two images are different.) The 20 ordinary amino acids in living things are in the "1" mirror im- age rather than the "d" (except in very old peptides that have had an opportunity to "racemize" or change chemically into the "d" form).

As a result of the great importance of these molecules, separate No- bel Prizes were awarded for the f'rrst automated quantitative analysis of the amino acids in a protein, the frost determination of the amino acid sequence of a protein, and the fmt determination of the three-dimensional structure of a protein. By 1960, it was obvious that a Nobel Prize would be awarded for the first synthesis of a protein (with tacit agreement that this would be an enzyme with at least 100 amino acid residues.) The problem was that no one could do this, including large laboratories with dozens of scientists and unlimited research budgets.

When you eat food, your digestive system breaks down the peptides in the food into the 20 amino acids. Then, in accordance with your own DNA codes, specialized enzymes and other molecules in your body reassemble these amino acids into peptides that you require for life. These specialized synthesis systems are very complicated.

In the laboratory, with current chemical techniques, three chemical reactions are required to create each peptide bond. For a 100 residue peptide, this is 300 reactions (plus a few others unique to the particular peptide). Each reaction involves dissolving the reactants in a suitable solvent under appropriate conditions, waiting for completion of the reaction, and then purification of the products. A 95% yield in each syn- thetic step would be considered excellent synthetic chemistry.

The yield after 300 such steps, however, would be 0.95 to the 300th power, which is 1/20,000,000. Therefore, one ounce of product would require over 600 tons of starting reactants - and enormous amounts of skill, since the synthetic and purification steps become increasingly difficult as the molecule becomes longer. Nevertheless, fame and for- tune beckoned, so in 1959 there were several large, well-funded research labs in the world racing to make the first enzyme.

Unfortunately for them (and fortunately for mankind), there was one man with almost no resources, but with a better idea. Dr. Merrifield reasoned that, if he attached the first amino acid in the peptide to a I large insoluble plastic bead (he ultimately used a polystyrene resin), he could build up the peptide without losses in the purification steps. Moreover, he believed that he could drive the synthetic reactions themselves to 99% or greater completion by appropriate adjustment of reaction conditions in the solvent surrounding the beads.

This idea was so revolutionary that Merrifield was ignored by most of the great peptide chemists of the day. Everyone knew, you see, that all of the reactants in a synthetic organic chemical reaction needed to be in solution before they would react completely. Merrifield's growing peptide-resin would be insoluble and therefore impossible to react quantitatively with the next amino acid. They neglected to realize that the inner and outer surfaces of the resin beads would effectively be in solution if the solvents were wisely chosen.

Over the next few years, Merrifield published a series of seminal papers - first, the synthesis of a four-residue peptide; second, the syn- thesis of the nine-residue hormone bradykinin; third, the total synthesis of insulin, which is comprised of two peptides totaling 51 residues; and, finally in 1969, the enzyme ribonuclease, which has 124 residues.

He accomplished these remarkable syntheses because he had not only a new idea, but also a unique set of personal characteristics that were well-suited to the task - brilliance, determination, hard work, and modesty. The latter was especially important because the development of a suitable set of reaction conditions in his new, unexplored field of solid phase synthesis required him to try and then discard nurnerous good ideas that less modest men would have pursued too long.

Near the end of the enzyme race, as the moguls of big-time science began to realize the value of Merrifield's techniques, there arose a danger that someone w ith vastly greater resources would simply adopt the solid phase idea and cross the finish line ahead of him. It happened, however, that those who tried this were beaten by their own immodesty. Each tried to alter the procedures to place his own intellectual stamp upon them. These alterations slowed them down.

Much more was contributed by Professor Merrifield than simply the first synthesis of an enzyme. He opened an entire new filed of synthetic organic chemistry - solid phase synthesis. This was especially important in biochemistry because so many of the biologically important molecules are specialized polymers.

Moreover, once the reaction products are insoluble, they can be physically trapped in various ways and the reactants and solvents simply pumped in and out by systems of suitable valves and pumps Therefore, the syntheses can be entirely automated, as was the first synthesis of the enzyme ribonuclease. Today, every issue of Science includes advertisements by various companies offering to custom synthesize macromolecules for scientists who do not have the appropriate automated apparatus. All of this is based on solid phase synthesis, with much of it still using Merrifield's original reaction conditions.

"Combinatorial chemistry" (mentioned above) is just one of many new fields that has arisen from this technique. In this field, molecular libraries are assembled and screened for molecules of special interest.

Suppose, for example, that a scientist has a 26 amino acid residue peptide with antibiotic (antibacterial) activity, and that he knows that four of the 26 residues are especially important to the activity. He would like to check the antibiotic activity of all 160,000 possible substitutions of the 20 amino acids at the four positions in order to synthesize the most effective antibiotic.

To do this, he synthesizes the peptide until he reaches the first of the four residues. At this point, he separates the resin into 20 portions and attaches a different amino acid to each portion. Then he recombines the portions and continues synthesizing until he come to the next of the four residues, whereupon the separation into 20 aliquots is again repeated, and so on. At the finish of the synthesis, the synthetic mixture contains all 160,000 different molecules with one important addition -each separate resin bead contains molecules with only one of the 160,000 sequences. The beads are then appropriately spread out, the peptides are partially released from the resin, and the surface is tested for antibacterial activity in such a way that the peptide can be recovered from any single resin bead portion showing high activity.

In this way, the peptide with maximum activity can be determined and then synthesized in large quantities for medical use. Suppose that, in the course of time, the bacteria develop a strain that is resistant to this peptide. In that case, the peptide library (the same one synthesized before) can be used to select another peptide with maximum activity against the new strain.

This method is already being used to develop new drugs as outlined in the R. F. Service article referenced above. With solid phase techniques, even very small laboratories with only a few employees can quickly develop custom-made new drugs and then produce them in limited, but commercially important quantities - acept that this is not permitted by our government. It places a more than $100 million dollar the Food and Drug Administration fine upon anyone wishing to improve public heaIth. Whether or not this money'is "for our protection" or is "protection money" we leave as an exercise for the reader.

Meanwhile, infectious diseases are not subject to FDA regulations See, for example, "Ominous Trends for Infectious Diseases" by Constance Holden, Science 272, p 1269 (1996).

Voila! You now have a vehicle approximating the new GM Impact electric car.

Move to an area with few hills and no snow.

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