Alphafold, a program developed by Google and the most important pan-European bioinformatics laboratory, will allow to examine in detail the three-dimensional structure of 200 million proteins, almost all of those known, opening the door to a new phase of studies and applications until now. unthinkable.
Thanks to the new space observatory James Webb Telescope, we are ready to observe very distant and massive objects. But to the surprises of this July 2022, unforgettable from the point of view of scientific research, another piece of news was added yesterday: thanks to an artificial intelligence program called Alphafold and thanks to a collaboration between Google and the most important pan-European bioinformatics laboratory, EMBL- EBI, since yesterday we can examine in detail the three-dimensional structure of very small objects very close to us, that is, 200 million proteins, almost all of them known to science.
In these pages, then, we announced the revolution that Alphafold promised: now that revolution has begun.
Let’s try to understand what happened, in a few words. I think we are all somewhat familiar with the idea that our genome, made up of DNA, determines how we are made. I deliberately use general terms, to approach the most widespread and common understanding. In fact, the genome of any organism, whether it is composed of DNA like ours or RNA like that of SARS-CoV-2, contains the instructions specified in its sequence to produce at the right time and in the right amount all the proteins that produce upload most of the machinery that is useful to make every living thing work. At the microscopic level, that is, we are a well-regulated set of billions and billions of proteins (from two to 4 million in a cube with a side equal to 1 millionth of a meter), whose stock (in the case of humans, a few tens of thousands of different types) stored in the genome of each cell. These proteins are the cogs, or rather machines of microscopic size, that with their functions, their precise three-dimensional structure and their chemical-physical properties allow every living thing to be what it is.
The simultaneous contraction of an astronomical number of copies of certain proteins contained in our muscles upon the arrival of a nerve impulse allows us to bend our arms. The binding of oxygen to another protein contained in our red blood cells allows this essential gas to be transported to every cell in our body. Still other proteins allow us to process the food we eat, from the ptyalin in our saliva to the enzymes in our stomach and the rest of our digestive system. specialized proteins, antibodies, bind and allow the destruction of pathogens. Other proteins, such as insulin, regulate the overall level of various molecules in our body. Still different proteins enable the transmission of nerve impulses at the synapses of our neurons. and so on, until we have completed the inventory of every single physiological function that enables us and every organism to live.
Just as in the case of a mechanic’s tools, the function that proteins can perform depends strictly on their shape, i.e. their three-dimensional structure. Seeing a screw go through wood, we understand what its helical groove is for. in the same way, to understand how a protein performs its function, it is necessary to examine its structure and how, during the protein’s activity, it acts on the surrounding environment. Furthermore, just as we can tell that a screw is broken by noticing that it is bent, in the same way that when we discover that a mutation of a piece of DNA leads us to produce a protein with the altered shape, we can infer that it will no longer function as it should. . this allows us to identify the mechanism behind many different diseases and to intervene by restoring the correct protein – for example replacing the defective copy of a gene, as in gene therapy, or providing the functional protein, as in the case of insulin for diabetics.
The problem is that, until now, obtaining information about the structure of a biological macromolecule has been a long and complex process: in 1957, Kendrew made known the structure of myoglobin, after 22 years of work, and despite remarkable progress, in the following 65 years, that is until today, the “shape” of approximately 190,000 proteins has been determined experimentally. Today, in one fell swoop, we have arrived at reliable information on 200 million proteins, which, I repeat, are almost all of those known. in one fell swoop, we see the “shape” of all the molecular machines, all the cogs that make up the cells and bodies of every living organism for which the genome has been determined.
A new era of unimaginable studies and applications has begun.