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A "bubble" per se would do no harm unless you have cells (without walls like mammalian cells) in the suspension. If you agitate the protein mixture vigourously then it may lead to denaturation of proteins by extensive intermolecular collisions. The "froth" formation is an indication of denaturation as denatured proteins stabilize these foams [1, 2]. ...


I would say impossible is a stretch. An inventive biochemist could create molecules that are "complimentary" to each amino acid similar to a Dna polymerase. Then a protein would be needed to both detect and translate this similarity into protein elongation. Unlikely, hell yes, impossible, no.


I suppose unligated oligonucleotide would also be "amplified" but on much lesser scale(?only one part of probe?). For instance after 6th run of PCR you would get 2^6=64 amplicons of ligated probe but only 6 for one unligated part(?second starter is designed to anneal to second part of antisense oligonucletide of probe?). After 30 runs there is massive ...

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