Good Enough for Now

Indeed.

That Doesn't Sound Very Sexy

Well, then, what about the mechanomeric selection of photoenzymes affording artificial photosynthesis of fuels, organic chemical industrial feedstocks, and bulk macronutrients, halting the alarming present-day massive industrial crustal-carbon fossil-fuel extraction and burning and consequent carbon dioxide emission and greenhouse warming; removing carbon dioxide from the atmosphere and "fixing" it into fuel and other stocks (not to mention all-but-eternal plastics), helping palliate the impact of previous extraction and burning and emission and warming; breaking the hold of the Fossil Fuel Cartel over the world, with its price-fixing, price-gouging and other corruption; and establishing the sustainable photosynthetic economy?

What Industrial Applications Are There for MeSe?

Many expensive and/or toxic and/or otherwise hazardous industrial chemical catalysts will be replaced by mechanomerically-selected enzymes.

Such enzymes will catalyze many reactions at lower temperatures and pressures than at present, lowering energy use and cost, and many others in water rather than more expensive and/or toxic and/or otherwise hazardous solvents.

Such catalysis due to enzymatic specificity will furthermore reduce side-reactions and increase the efficiency and economy of such reactions.

And it will also allow new reactions to be developed and run as well, such as higher-order ones involving greater numbers of reactants at a time.

Can Oncotherapeutic (Anticancer) Mechanomers Be Mechanomerically Selected?

Mechanomers toxic to cancer cells but not to cells of their parent (or other normal) types can be mechanomerically selected, for the individualized oncotherapies or idiotherapies necessitated by the individualized nature of cancers.

Cancer cells are mutated cells, with at least one and usually multiple abnormal biopolymers (DNAs, messenger RNAs and proteins), and the differences between such biopolymers and their normal parent biopolymers will allow the mechanomeric selection of mechanomers which are toxic to such cells only (e.g., lethal enzymes activated by complexing with such abnormal biopolymers only).

At its simplest, such selection will take the form of parallel matricial mechanomeric selection: overlaying a set of parallel identical replicated random mechanomer matrices with, respectively, a culture of the cancer cells in question, perhaps a culture of the parent cell-type of that cancer, and cytopalette cultures of as many other (normal) cell types generated and cultured from the patient as practicable; observing for regions where on the first matrix the cancer cells die but on the others none do, deaths signaled by mechanomeric indication for greatest sensitivity; extracting the random mechanomers from those regions from yet another parallel matrix; re-matriciating the mechanomers from each such region using different media to separate them; and repeating, until a set of individualized antineoplastic or oncotherapeutic mechanomers is selected.

It is unlikely that even with the use of multiple oncotherapeutic mechanomers that all the cells of a cancer will be killed, and indeed some if not most cancers more or less steadily mutate, so the mechanomeric oncotherapies of such cancers will therefore involve not only multiple mechanomers but also one or more extra passes or rounds of such multiplex therapy, as the cancer reoccurs to be re-sampled and a new set of oncotheraputic mechanomers selected to deal with it, with the majority of such cells destroyed by each pass, and a genetically-different minority left (if any) to begin again (note that even if not directly destroyed, the cells of such cancer held in check long enough should become ever more mutated, function ever more poorly, with ever greater numbers of its cells being fatally mutated, or exhibiting mutated biopolymers detectable and those cells therefore destroyed by the immune system, in "neoplastic burnout").

Can Mechanomeric Antivirals Be Mechanomerically Selected?

Mechanomers preventing viral destruction of cells can be mechanomerically selected.

At its simplest, such selection will take the form of parallel matricial mechanomeric selection: overlaying a set of parallel identical replicated random mechanomer matrices with, respectively, cytopalette cultures of as many different human cell types from as many different humans as practicable, and cultures of human microbial commensals (to avoid for example disturbing normal human gastrointestinal microflora and possibly facilitating fulminating toxic overgrowths); overlaying the human cell matrices with a solution of the virus in question; observing for regions where on the human cell matrices the cells do not die but on the microbial matrices no cells do, deaths signaled by mechanomeric indication for greatest sensitivity; extracting the random mechanomers from those regions from yet another parallel matrix; re-matriciating the mechanomers from each such region using different media to separate them; and repeating, until a specific and effective antiviral is developed.

Note that such antiviral selection is even more flexible than viral development of resistance to antivirals, since mechanomeric selection of antivirals is limited neither to starting from naturally-existing mechanomers nor to mechanomers of naturally-existing classes.

Furthermore, it will be much faster than the viral development of antiviral resistance.

Can Mechanomeric Antibiotics Be Mechanomerically Selected?

Mechanomers specifically toxic to microbes of a given species but not to those of other species or to humans can be mechanomerically selected.

At its simplest, such development will take the form of parallel matricial mechanomeric selection: overlaying a set of parallel identical replicated random mechanomer matrices with, respectively, a culture of the microbes in question, cultures of microbes of as many other species as practicable, both human commensals (to avoid for example disturbing normal human gastrointestinal microflora and possibly facilitating fulminating toxic overgrowths) and a selection of environmentally-significant species, and cytopalette cultures of as many different human cell types from as many different humans as practicable; observing for regions where on the first matrix the microbial cells die but on the others no cells do, deaths signaled by mechanomeric indication for greatest sensitivity; extracting the random mechanomers from those regions from yet another parallel matrix; re-matriciating the mechanomers from each such region using different media to separate them; and repeating, until a specific and effective antimicrobial is developed.

Note that such antimicrobial selection is even more flexible than microbial development of resistance to antimicrobials, since mechanomeric selection of antimicrobials is limited neither to starting from naturally-existing mechanomers nor to mechanomers of naturally-existing classes.

Furthermore, it will be much faster than the microbial development of resistance to antimicrobials.

Mechanomeric Selection Should Be Useful

The utility of mechanomeric selection is highlighted by its applications to itself in mechanomeric indication, mechanomeric evolution, mechanomerogenesis and other early mechanomeric selection including the development of cytopalettes.

Will Any Other Mechanomers Be Useful for Mechanomeric Selection?

Sets of mechanomers—growth hormones stimulating cell reproduction and cytodifferentiators converting cells of a sample type to those of others—will be developed and refined and expanded which allow construction of cytopalettes, sets of cultures of cells of different types, for use in matricial mechanomeric selective matricial overlays in parallel testing of mechanomers for toxicity (including environmental safety). Cytopalettes will include multicytotypic such as neuromuscular junctional cultures. Cytopalettes cultured from cell samples from individual patients will allow the custom selection of mechanomeric pharmaceuticals for use in idiotherapies, individual or customized therapies of refractory infections and idiopathic diseases, including cancers. And such cells and tissues will be used for replenishment and replacement, and the engineering of organs for (more or less) autotransplantation. And mechanomeric indicases or indicating systems should be developed for use with cytopalette cultures to indicate cell death and disfunction.

Where Will We Get the Enzymes Needed for Mechanomeric Selection?

The mechanomeric selective enzymes and other mechanomers will themselves be mechanomerically selected, in what is called here "early mechanomeric selection":

Replication being a more complex function than and indeed including polymerization, replicases must be more complex and therefore occur more rarely in random mechanomer stocks than polymerases, but cross-class replicase pairs, one from each of two mechanomer classes replicating mechanomers of the other, will evolve in what is called here "mechanomerogenesis" (analogous to abiogenesis), in which random mechanomers and monomers of both classes are mixed, and such replicases upon encountering one another engage in a more or less exponential course of mutual replication (with a more or less exponentially-increasing heat of replication), with the first such event and pair likely taking over the system. Many such events will produce same-class pairs, which pairs will also limit mechanomeric evolutionary system sizes, and many cross-class replicases produced will be incapable of replicating mechanomers incorporating monomers of all the kinds of the appropriate class supplied, and more or less inaccurate or fuzzy in their replication of the mechanomers they can replicate (such reduced-monomer-set replicases will often be workable until better ones are developed, and such fuzzy replicases will be useful for increasing the incidence of well-conformed mechanomers in random mechanomer stocks).

Once a workable replicase pair is developed, at least one polymerase of each class polymerizing monomers of the other will be developed by matricial mechanomeric selection, using random mechanomers synthesized by purely-chemical (non-enzyme-catalyzed) polymerization and then replicated. Such polymerase pairs must operate in the same directions as their classmate replicases, although replicases and polymerases operating in both directions will be developed to mechanomerically select mechanomers which in the course of synthesis coil in such ways as to bury the ends first synthesized and prevent replication, as well as those which vary in their conformations depending on direction of synthesis.

Will There Be Any More Advanced or Powerful Methods of Mechanomeric Selection?

Mechanomeric evolution, freely mixing unreplicated random mechanomers and monomers with a replicase complexed with a previously-mechanomerically-selected conditional replicase inhibitor which inhibits replication except under some condition resulting from the performance of the desired mechanomeric function, will test the greatest possible number of random mechanomers at a time for a desired function and therefore facilitate the development of mechanomers performing more complex functions and therefore occurring more infrequently in random mechanomer stocks. Mechanomeric evolutionary system sizes will be limited by same-class replicase-pair takeovers, and in such selection of any mechanomer the function of which is more complex than that of a mechanomer disinhibiting the replicase, false evolutions will outnumber true.

Mechanomeric Indication Should Be Useful in Many Other Contexts than Empirical Mechanomeric Developmental Matricial Analysis, Shouldn't It?

Yes, mechanomeric indicases or indicating systems should comprise one of the largest classes of mechanomerically-selected mechanomers, for use in science, engineering and medicine.

How Will Mechanomers Performing Desired Functions Be Detected in the Matrix?

Matricial analysis will of course use infrared spectroscopy and nuclear magnetic resonance imaging where appropriate. It will also use orthogonal analysis, by orthogonalization or third-dimensional separation of the matrix, for example by blotting the matrix into one end of and separating its components using a very wide chromatographic column (and orthogonal standards inoculated into the margin of the original square matrix marking in the orthogonal matrix or column planes or bands of interest). But matricial analysis will above all use mechanomeric indication, overlaying the matrix with a previously-mechanomerically-selected enzyme, an indicase, which under some condition resulting from the performance of the desired mechanomeric function catalyzes a reaction causing a color-change on the matrix. Such technique by its analysis at the molecular level, analysis by complexing, cumulative indication as colored indicator accumulates, and ability to use the product of one indicase to trigger another to amplify indication, will render most mechanomeric selection amenable to being performed as matricial mechanomeric selection. In such selection of any mechanomer the function of which is more complex than that of a simple enzyme catalyzing the indicating reaction, false indications will outnumber true, so multiple indicases should be developed and used to signal both true and false positives.

Matriciation Should Be Ordered, Shouldn't It?

Matriciation must be ordered—for example by affine chromatography, chromatographing a sample of a replicated random mechanomer stock using one chromatographic medium and blotting the resulting linear chromatogram into one side of a different medium and chromatographing that a right angle to the first, forming a square or two-dimensional matrix, perhaps itself blotted into a final test matrix and medium—to localize the replicands and effects of each different mechanomer in its characteristic location on the matrix, maximizing concentration of effect and minimizing gestation time (time for effect to accumulate to detectability) and analytical sensitivity needed; to perform parallel testing of mechanomers under different or incompatible conditions, using identical matriciations of multiple samples of a replicated random mechanomer stock and comparing mechanomer behaviors at their identical locations from matrix to matrix; to perform parallel recovery of mechanomers from a matrix parallel to a test matrix from which it would be difficult or impossible to recover the tested mechanomers; and to separate most mechanomers and therefore decrease mechanomeric interactions on and in the matrix, causing enzymes degrading mechanomers of their own class to preferentially degrade their own replicands.

How Will These Random Mechanomer Stocks Be Tested for Mechanomers Performing Desired Functions?

Matricial mechanomeric selection, analogous to antibiotic sensitivity testing, will be the simplest and most common form of such selection, at its own simplest matriciating (spreading and arraying) a sample of a replicated random mechanomer stock across or through or into a thin layer; overlaying that matrix with any materials and subjecting it to any other conditions needed for the desired function; analyzing the matrix identifying locations in which the desired function is being performed; extracting the mechanomers from those locations for further replication and testing, perhaps by another round of such development (using a different matriciation to redistribute the mechanomers in the sample); and replicating the mechanomer finally selected for its performance of the desired function for production.

Will Random Mechanomer Stocks Be Stable?

Depolymerases and other enzymes degrading mechanomers of their own class will occur in every random mechanomer stock and make it unstable. Such reactions and enzymes for the most part will be simple ones, the collective incidence of such enzymes in such stocks will be correspondingly high, such stocks will be correspondingly unstable, and such problems will be exacerbated by replication. Random mechanomer stocks should therefore be freshly prepared for mechanomeric selection. But if such stock must be stored it should be kept cold, decreasing reaction rates in general; dry, if depolymerization incorporates solvent into the free monomers, as with proteins, amino acids and water; and matriciated, separating most mechanomers in the stock and causing degradative enzymes to preferentially degrade their own replicands.

What Range of Gestations or Developmental Times Are We Talking About Here?

Ten thousand random proteins three hundred amino acids in length will collectively mass a little over six hundred attograms, which stock if replicated to one gram will average about 1.6 quadrillion replicands and one hundred micrograms of each protein, which replicands if of an enzyme each molecule of which produces ten product molecules per second each with the mass of an amino acid will take about four and a half minutes to produce one milligram of such, while one trillion such proteins will mass a little over sixty nanograms, which replicated to one gram will average about sixteen million replicands and a picogram of each, which as such enzyme will take about ten months to produce one microgram of product.

How Frequently Should Mechanomers Exercising Desired Functions Occur in Well-Conformed Random Mechanomer Stocks?

Proteins vary widely in the numbers and orders of the amino acids of which they are composed, but three hundred amino acids is a typical natural protein length and size, and if all proteins with all possible amino acid orders of that length were synthesized, the total mass of protein synthesized would be several hundred powers of ten times the mass of our galaxy. Plainly, if each and every protein function could be performed by only one specific protein with one specific amino acid order, no biological process or artificial procedure could ever develop such. But the evolution of proteins and other mechanomers, and the development and function of antibodies in the body, and vaccination and the development and use of antisera and monoclonal antibodies, all prove not only that mechanomers with different monomer orders can share a given function but that there must be a fantastically high degree of coincidence of function among them. Hundreds out of the millions of different antibodies in the body typically complex with a given antigen, which incidence of one in ten thousand is taken here to be that of such simplest function among well-conformed random mechanomers (taking the restriction of antibody complexing to its antigen binding site alone to cancel out multiple antibody complexing of different parts of antigen). And the greater the number of functions performed by a mechanomer, and the greater their complexities, the lower will be such incidence of such mechanomer, the incidence with two sites performing such functions taken here to be about one in ten thousand squared or one in one hundred million, and the incidence with three one in ten thousand cubed or one in one trillion.

Is There Anything Else to the Synthesis of These Random Mechanomers?

Proteins generally each assume a single stable conformation, or change between two or three conformations by way and in course of function, but perhaps fewer than one in one billion random amino acid orders specify such well-conformed proteins, and such incidence is taken here to be that of well-conformed mechanomers in random mechanomer stocks. Many mechanomeric functions might be performed by mechanomers which do not assume such conformations (if only because conformed by complexing in course and by way of function), and such incidence will be adequate for the mechanomeric selection of mechanomers performing the simplest functions anyway, but selection of mechanomers performing more complex functions will require use of some technique(s) for increasing such incidence. Three such techniques, in order of increasing complexity and decrease in synthesis of poorly-conformed mechanomers, are diagonalization (chromatographing random mechanomers along one side of a square medium or matrix and then at a right angle to the original direction until the spectrum lies largely along and is enriched in well-conformed mechanomers along the diagonal, well-conformed mechanomers being more sharply localized in chromatography, such mechanomers extracted and the procedure repeated, using different media), fuzzy replication (using an inaccurate or fuzzy replicase to replicate an original well-conformed mechanomer, perhaps with a function similar or even identical in part to that desired, and synthesize a random mechanomer stock, analogous to evolution), and splicing (of random or fuzzily-replicated segments into the appropriate areas of otherwise well-conformed mechanomers, analogous to antibody antigen binding site development, followed by replication to insure that those mechanomers assume the conformations they would have assumed upon continuous polymerization and will upon replication for production).

Where Do We Get These Mechanomers?

Random polymerization of a mixture of monomers of the different kinds of the appropriate class will produce a mixture of different random mechanomers of the desired class, a random mechanomer stock, and replication or molecular copying of the mechanomers in such stock a mixture of many replicands of each of those mechanomers, a replicated random mechanomer stock. Such stocks will be the fundamental tools of mechanomeric selection. And such polymerization and replication will be catalyzed by enzymes, at least one polymerase and replicase respectively, both of another class of mechanomer than that of those being synthesized to avoid unwanted operations upon those enzymes themselves, both operating in the same direction along and continuously upon the growing mechanomer during its synthesis to insure that the replicands have the same conformations as the original, and both themselves mechanomerically selected, in early mechanomeric selection.

So We Can Mechanomerically Select Proteins?

Nucleic acids should not be mechanomerically selected, to prevent unwanted genomic introductions. Mechanomer classes mechanomers of which are to be mechanomerically selected should not use naturally-existing monomers, to prevent naturalizations of replicative systems. And mechanomers of classes mechanomers of which are to be mechanomerically selected should be non-toxic and biodegradable.

Prove It

Mechanomers are developed in nature by variation of monomer order—and therefore of conformation, and therefore of shape, mechanical properties and surface structure, and therefore of function—followed by selection.

Evolution's scale, in numbers of mechanomers and selections and in time, keeps it from being proof that mechanomeric selection is practicable; but the development of each individual's antibody (protein) complement, and still more each duck's in the egg, and still more the primary immune response, and most of all vaccination and the development and use of antisera and monoclonal antibodies, furnish so many everyday small-scale proofs that proteins performing such more or less simple complexings or molecular recognitions as antibodies can be mechanomerically selected. Enzymes being so many more examples of such complexings can therefore be selected likewise. Proteins performing any equally simple functions or small combinations thereof likewise. Nucleic acids likewise. And mechanomers of other classes likewise.

Can We Develop Mechanomers to Perform Desired Functions?

Mechanomers performing desired functions, such as enzymes and molecular machines, can be selected from among random mechanomers, mechanomers with random monomer orders, and therefore random conformations, and therefore random shapes, mechanical properties and surface structures, and therefore random functions, in what we call here "mechanomeric selection" (abbreviated "MeSe", and pronounced "meh-seh" if need be).

Why Are We Talking about Proteins Again?

We take proteins, the workhorses of the living cell, to be the type or classic mechanomers and biopolymers.

How Do Proteins Function?

Two proteins or other large molecules of complementary shape and surface charge-patterns upon being brought together will develop multiple attractions including hydrogen-bonds to one another, such fit and collective attraction being called an affinity and such collective bond a complex.

Protein complexing is so generally specific in its requirements of complementary shape and charge-pattern as to be described as “lock-and-key”.

And protein complexing is a fundamental mechanism of protein function:

The conformation-determining attractions and bonds of and within the protein itself can be considered intramolecular or internal complexing.

Cytostructural proteins complex with one another to form the internal structural framework of the cell called the cytoskeleton.

And every cell contains protein enzymes catalyzing—accelerating—the chemical reactions used by that cell, which reactions would otherwise run too slowly to be of use:

Body cells typically each synthesize thousands of different enzymes, and many molecules of each, each more or less specifically catalyzing its specific reaction operating upon its specific substrate(s) or reactant(s) (the phrase "lock-and-key" was first applied to enzyme specificity). And each enzyme catalyzes its reaction largely through, and its specificity is that of, not so much its complexing with its substrate(s) as with its reaction's rate-determining transition state, the highest-energy state through which that reaction must proceed, stabilizing and therefore lowering the energy of that state, allowing lower-energy passage through that state, increasing the probability that a given enzyme-substrate complex will have the energy needed to pass through that state, and therefore, in the cell or other reaction mixture where many such complexes are forming and dissociating, increasing the number of such able to pass through that state and their reactions proceed to completion at any given time, and therefore the overall rate of reaction.

In addition, many enzymes catalyze water-sensitive reactions in their hydrophobic cores.

More complicatedly, many if not most proteins function by virtue of conformation changes, changing back and forth between two or more conformations in the course and by way of function, a phenomenon called allostery, and complexing is frequently combined in protein function with allosteric conformation changes. Protein complexing of one molecule causing an allosteric conformation change in that protein enabling or preventing subsequent complexing of another molecule is a central mechanism of protein function and control in the cell; for example, some enzymes, including some acting as cell switches, sensors or governors, are activated or deactivated—turned on or off—by conformation changes caused by complexing with or dissociating from the appropriate molecules, some used specifically as signals. And other protein enzymes catalyze the degradation of fuel and use the energy yielded to repetitively alter their conformations and shapes, acting as motors and machines.

Does Protein Conformation Matter?

Protein conformation determines protein shape, whether globular, elongated or flattened, and whether solid, indented or hollow; protein mechanical properties, such as whether and how one part of a protein can bend or rotate with respect to the rest; and protein surface structure, the protein’s surface shape and pattern of exposed side-groups and backbone units.

Do Protein Amino Acid Orders Matter?

Proteins can rotate around their backbone single bonds, and therefore all along their backbones, and consequently twist and coil, but the proteins which perform the functions of the cell generally assume three-dimensional coiled structures or conformations specific to their kinds, stabilized in various ways.

For example, attractions between positively- and negatively-charged moieties of molecules form what are called hydrogen bonds, which separately are weaker but collectively can be much stronger than any one molecular bond.

Such bonds between nearby backbone units along the protein backbone cause the assumption of winding or helical conformations along the backbone, as well as sheet conformations involving multiple turns and side-by-side runs thereof. Such interactions and resulting conformations are not specific to any particular protein or moiety thereof, since every backbone unit is identical to and can form the same such bonds as any other, and any stretch of backbone could theoretically engage in any such conformation.

Slightly more specifically, the backbone units and some side-groups hydrogen-bond water molecules, and proteins tend to coil in such a way as to present such water-soluble or hydrophilic moieties or groups on their surfaces, and hold those side-groups which cannot form such bonds inside, in water-insoluble or hydrophobic cores.

But in most of the proteins which perform the functions of the cell, conformation is specified by side-group interactions, which depend on the kinds of side-groups available and the order in which they occur, which depend in turn on which amino acids are incorporated into the protein and the order in which they are incorporated.

That is, protein amino acid order determines protein conformation.

How Big Are Proteins?

Proteins of different kinds and functions vary widely in the number of amino acids of which they are composed.

But three hundred amino acids is a typical natural protein length and size.

And a typical average natural protein mass can be calculated based on that length and size by multiplying the average mass of an amino acid (see "What Are the Protein Monomers") times three hundred, and then subtracting the combined masses of the two hundred and ninety-nine water molecule equivalents lost ("What Are the Protein Monomers"), amounting to about 6.16 * 10^-20 gram, about sixty zeptograms, a little over two thousand times the mass of a water molecule.

And the corresponding typical average natural protein gram number, the number of such proteins contained in one gram thereof, can be calculated by dividing that mass into one gram, giving about 1.62 * 10¹⁹ or about sixteen quintillion such proteins per gram.

How Do Their Amino Acids Fit into Proteins?

The invariant moieties of the amino acids incorporated into a protein, minus water of polymerization, comprise what is called its backbone, an elongated and repetitive structure in which each invariant moiety remnant incorporated forms a unit identical to every other (although of course the end-units each bear a free bonding group unused in polymerization).

And the prosthetic groups of those amino acids become protein side-groups projecting from those protein backbone units and that backbone.

What Are the Protein Monomers?

Proteins are synthesized from monomers called amino acids, of which there are twenty different kinds.

The amino acids are small molecules, composed of only ten to twenty-seven atoms each, depending on kind, averaging about twenty, and averaging in mass about 2.35 * 10^-22 gram, about one-quarter of one zeptogram (sextillionth of a gram), or 235 yoctograms (septillionths of a gram), about eight times as much as the three-atom water molecule, an oxygen atom single-bonded to each of two hydrogen atoms (an oxygen atom forms two single bonds or one double bond in a molecule, while a hydrogen atom forms one single), the total mass of which is about 2.99 * 10^-23 gram, or thirty yoctograms.

Every amino acid molecule consists of a central carbon atom single-bonded to a hydrogen atom, an amino group, a carboxylic acid group and a prosthetic group (a carbon atom forms four single bonds in a molecule, or one double bond and two singles, or two double bonds, or one triple bond and one single).

An amino group is composed of a nitrogen atom (which forms three single bonds, or one double and one single, or one triple) single-bonded to each of two hydrogen atoms.

And a carboxylic acid group is composed of a carbonyl group or moiety, a carbon double-bonded to an oxygen atom, further single-bonded to a hydroxy or alcohol group, an oxygen atom single-bonded to a hydrogen atom.

Such bonds and groups are of course the ordinary molecular bonds and functional groups of carbon chemistry, called "organic chemistry" due to life's taking such advantage of the ability of carbon to form large and stable molecules that all carbon on the face of the earth is or has been part of a living organism.

And the amino acid amino and carboxylic acid groups are of course what gives it its name.

Every amino acid is identical to every other in the above, regardless of kind, in a nine-atom moiety called here its invariant moiety, composed of its central carbon atom and the hydrogen atom and amino and carboxylic acid groups bonded to it.

And an amino acid of one kind differs from one of another solely in the elemental composition (the kinds and number of atoms involved), structure (how those atoms are bonded together) and consequent properties of its prosthetic group.

Are Biopolymers Important?

Living organisms are composed of cells, and most cell structures are formed or synthesized and most other cell functions are performed by the mechanomers and biopolymers called proteins.

Each such function is performed by its own particular and specific protein, or set thereof, and usually many molecules of each.

And a body cell typically synthesizes and uses tens of thousands of different proteins.

Are There Natural Mechanomers?

The natural mechanomers, which we distinguish as "biopolymers" when needed, include proteins, nucleic acids and polysaccharides.

Can We Make Polymers?

Plastics, simple artificial structural polymers composed of monomers of only one or two kinds, are ubiquitous.

What Are Polymers and Monomers?

Polymers are molecules synthesized by the chemical bonding together or polymerization of many other molecules called their monomers.

What Are Copolymers?

Copolymers are polymers composed of monomers of more than one kind.

What Are Mechanomers?

Mechanomers are functional copolymers.

What Is MeSe?

MeSe stands for "Mechanomeric Selection", the selection of mechanomers performing desired functions, such as enzymes and molecular machines, from among random mechanomers.