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Prior to the current study the process from cutting to joining was not understood.
Researchers from The University of Western Australia and the University of Minnesota have at last provided a structural explanation of how sunflowers make super-stable protein rings and by inference, how the many other plants with circular proteins also do this. The study determined the crystal structure of an active form of the enzyme AEP from sunflower seeds.
“Super-stable peptides like these PLPs are thought to represent the next generation of drugs and we have just found dozens of them and they’re unlike anything seen before,” Mr Fisher said.
They are so small, they hardly behave like proteins at all.
“Now we have so many of them in our hands, it’s time to work out why plants are making so many different ones in their seeds.
“For a long time, proteins this tiny were assumed to be assembled like LEGO, one amino acid block at a time.
We’ve shown they are chopped out of much larger proteins encoded by genes.