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How Did the Three-Dimensional Structures of Proteins Evolve in Nature?

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Lupas,  Andrei N.
Max Planck Institute for Developmental Biology, Max Planck Society;

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Citation

Lupas, A. N. (2016). How Did the Three-Dimensional Structures of Proteins Evolve in Nature? doi:10.21036/LTPUB10264.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002B-BBC1-3
Abstract
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.