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Saturday, 31 October 2020

Make me a monster

Is science on the verge of building a real Frankenstein’s monster?
 
Frankenstein made his monster in his laboratory through techniques he never revealed. Christian Michaud (Victor Frankenstein) et Étienne Pilon (La Créature) via Wikipedia Commons.

Well, with recent advances in protein design[1], the possibility of growing new organs and limbs in labs may not be as far away as we imagined.

Proteins; big, long, complicated molecules, folded precisely to assist them with their function. They’re an essential for coding life, building our bodies and directing our processes. They’ve long given biochemists the runaround, but the quest continues to understand how design links to function and to build new proteins to aid health, energy, environmental and food sciences.

Every time I read Frankenstein I wonder – what could Frankenstein’s method have been? How did he connect up the graverobbed bodyparts to make his new human?
Shelley's novel. Drümmkopf (Flikr).

There isn’t a natural protein that helps us with the complexity of this challenge – in fact, there aren’t proteins to do many of the simpler jobs we want (or, at least, we haven’t found them). Today, scientists can adjust existing proteins to exaggerate different functions, but de novo protein design – design from scratch – remains the unrealised holy grail.

Recent advances, however, have taken us a big step closer to the “human building” possibilities that haunted Mary Shelley and inspired her famous novel[1].

Why is it so complicated?

Proteins are big. Polymers of amino acids, they’re sometimes 10 or 20 in length, and other times 1000s. Since there are 20 different amino acids, there are 20 possibilities for each position in the chain, meaning that even if you account for symmetry, there are more than 5000 billion (20 to the power of 10 divided by 2) possibilities. Yeah. So just making them and testing them is not an option. Not only this. The way proteins fold affects their behaviour. And there are so many possibilities for how chains could fold up. Too many for our computers to handle, so even computer modelling is unable to make a significant dent in the world of protein possibilities.

However, new work on structure prediction in protein folding and de novo protein design has uncovered ways to limit the possibilities by classifying methods, and putting in some of the ways we have to build proteins right now, such as using different templates[1]. This means there are far fewer proteins to potentially make and to study – not necessarily the best ones, but at least it’s headway.

Soon, we might be able to use the “brute force method” to make some useful proteins, and to use them transform life itself.

...Happy Halloween!

References
why don't all references have links?

[1] Floudas, C. A., et al. Advances in protein structure prediction and de novo protein design: A review. Chemical Engineering Science 61.3 (2006): 966-988. doi:10.1016/j.ces.2005.04.009.

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