In my blogs of last week and the week before, I discussed the use of evolutionary methods for improving biotechnological processes. I have also blogged, more than once, about the concept of the economy as an evolutionary ecosystem. The question then arises as to whether the development of technology in general might be seen in this way. While it is clear that minor improvements in existing products or technologies can be seen as ‘evolutionary’ advances derived from their ‘parents’ or precursors, it is not so clear how this metaphor might be applied to the arrival of novel and disruptive technologies that have no obvious precursors. That the evolutionary metaphor does work is the theme of a new book by Brian Arthur. The chief recognition is that all kinds of complex products (and these can include ‘products’ like musical symphonies!) arise largely by the combination or recombination of existing modules. These existing components may also provide novelty by processes akin to horizontal gene transfer, something that genome sequencing methods have shown us is far more common than was previously anticipated.

Now, some of these general ideas have been promoted by writers such as David Goldberg, John Koza and Stuart Kauffman, but Arthur provides a particularly readable, eloquent, coherently argued and up-to-date overview.

I tend to have a penchant for ideas and discoveries that seem to (or do) come from left field, and one that came my way this week (illustrating some of the points about novel technologies, above) was the production of the first liquid protein (or protein liquid). Now while we recognise proteins as solids, as components of colloidal aqueous (and organic) solutions, and even (inside mass spectrometers) in the gaseous phase, no one had (apparently) previously made a liquid from a pure protein (derivative) with no added solvent. Indeed, there are fundamental biophysical reasons why this is hard, since the dimensions of protein molecules typically exceed the range of their intermolecular forces, such that liquid–vapour co-existence is unattainable. To overcome this, one way would be to modify the  surface properties of the protein to increase the range of the intermolecular force field to a length scale greater in size than the protein molecules, thereby enabling thermally induced molecular motions to be correlated over extended distances (i.e. to provide liquid-like behaviour).

Based in part on experiments of Giannelis and coworkers with inorganic nanostructures, this is what Mann and his colleagues at Bristol have now done, using a derivative of the iron-binding protein ferritin. It is early days yet, but the methods they use seem fairly general, albeit more favourable for spherical molecules like ferritin, and – given that there are enormous numbers of possible proteins – one can at least imagine many uses to which a protein liquid might be put. No doubt the exponents of molecular gastronomy are <ahem> licking their lips.

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