In a bacterial strain, antibiotics bind to the ribosomes, preventing them from making the proteins the bacteria need to survive.
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She has succeeded in determining the structure of ribosomes and the way in which antibiotics disrupt these.
They are, nevertheless, relatively large by cellular standards three times the size of ribosomes (the factories that produce proteins).
The researchers therefore synthesised messengers corresponding to the various versions of the ancient gene, fed them to some ribosomes, and collected the proteins that came out.
When they mixed their artificial biochemicals (including the unnatural amino acid) with a bacterial extract that contained ribosomes and all the appropriate enzymes, Dr Hirao and Dr Yokoyama found that the unnatural additions were treated just like their natural analogues.
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This knowledge can be applied to improving the ability of antibiotics to target ribosomes of pathogens, helping to combat the problem of resistance.
As this ring moves along the rod, it picks chemical units and assembles them into chains, just as ribosomes join up the building blocks of proteins.
The genetic code contained in the DNA is read by ribosomes in chunks of three individual components.
Ribosomes are a key target for antibiotics, as antibiotics are able to attack the ribosomal activity of harmful bacteria while leaving human ribosomes untouched.
Ribosomes are responsible for the production of all proteins in living cells, including those of humans, plants and bacteria.
Yonath's research has also revealed the precise modes of action of over 20 different antibiotics targeting bacterial ribosomes, shedding light on how bacteria become resistant to antibiotics.
It was a stretch of DNA that could be transcribed by an enzyme called polymerase into a chemically similar molecule known as RNA. The RNA acted as a messenger that was itself translated into protein molecules in sub-cellular factories called ribosomes.
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