True continuous bonding also provides for a good condition for directed organismic growth under tractive-, pressure-, and strain effects (already effective in the embryological development), as well as [providing a good condition] for the possibility of fibre formation, fibers, that are very effective in, and to be used in, mechanical support- and form-elements.
The facts of thermal coagulation and of denaturation, and the existence-only in a very particular electrolyte medium, demonstrate that the bioproteins, as long as they are capable of functioning, display a completely determined mesomeric structure [I presume a structure containing mediating elements] or a reversible manifold of such a structure, whereas if not having it, are not true bioproteins anymore. They then, generally, turn into the "normal" proteins, and thus then being not identical or even comparable with living bioproteins. No already developed or surmised views [and methods] will do in determining the exact nature of these living proteins, and there is good reason to base the one-off nature of life also on the one-off connection-relations, one-off interaction-relations, or one-off resonance-relations among the protein constituents. Of all known lower chemical building-blocks [together making up proteins] at least the amino acids are most appropriate to form the demanded combinations. For instance, the symplex- or cenapse formation [I presume : synapse formation] ( protein + lipoid or fatty acids, or, generally : compounds of proteins with other molecules) is a special case of a very common principle.