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Proteins mediate a vast array of functions in the body, like fighting invaders or transporting oxygen. Their remarkable properties are due to their three-dimensional structure which is acquired by a simple chain of molecules, a polypeptide, folding into a complex structure, the protein. This folding process is still not fully understood and hence also difficult to replicate in a laboratory. To learn more about how it works the research presented by ANDREI N. LUPAS in this video looked into the evolution of folded proteins. By comparing protein sequences, they identified common ancestors and found simple processes, such as repetition, are instrumental in allowing these to yield folded proteins: By repeating peptides in molecule chains, the researchers managed to create polypeptides that folded into proteins with a high success rate.
DOI:
https://doi.org/10.21036/LTPUB10264
Institution
Max Planck Institute for Biology Tübingen
Basic research at the Max Planck Institute for Biology Tübingen addresses fundamental questions in microbial, algal, plant and animal biology, including the interaction between different organisms. The approaches we use range from biochemistry, cell and developmental biology to evolutionary and ecological genetics, functional genomics and bioinformatics. The institute currently has five active departments, each led by a Director
Original publication
A Vocabulary of Ancient Peptides at the Origin of Folded Proteins
eLife
Published in 2015
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