Thursday, February 17, 2011
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).