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

Andrei N. Lupas

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

Researcher

Andrei N. Lupas is Director and Scientific Member at the Max Planck Institute for Developmental Biology. Between 1985 and 1990 he studied molecular biology at Princeton University (USA), where he received his PhD in 1991. In his research, Lupas concentrates on the evolution and classification of proteins, one of the essential building blocks of living cells. Lupas seeks to understand the folding process of the three dimensional structure which makes up the protein.

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