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  More than the sum of their parts: on the evolution of proteins from peptides.

Söding, J., & Lupas, A. N. (2003). More than the sum of their parts: on the evolution of proteins from peptides. Bioessays, 25(9), 837-846. doi:10.1002/bies.10321.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0017-ED1F-4 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-C5A5-E
Genre: Journal Article

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1944254.pdf (Publisher version), 376KB
 
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 Creators:
Söding, J.1, Author              
Lupas, A. N.2, Author
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1Research Group of Computational Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1933286              
2external, ou_persistent22              

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 Abstract: Despite their seemingly endless diversity, proteins adopt a limited number of structural forms. It has been estimated that 80% of proteins will be found to adopt one of only about 400 folds, most of which are already known. These folds are largely formed by a limited ‘vocabulary’ of recurring supersecondary structure elements, often by repetition of the same element and, increasingly, elements similar in both structure and sequence are discovered. This suggests that modern proteins evolved by fusion and recombination from a more ancient peptide world and that many of the core folds observed today may contain homologous building blocks. The peptides forming these building blocks would not in themselves have had the ability to fold, but would have emerged as cofactors supporting RNA-based replication and catalysis (the ‘RNA world’). Their association into larger structures and eventual fusion into polypeptide chains would have allowed them to become independent of their RNA scaffold, leading to the evolution of a novel type of macromolecule: the folded protein.

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Language(s): eng - English
 Dates: 2003-09
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1002/bies.10321
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Title: Bioessays
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Source Genre: Journal
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Publ. Info: Cambridge, UK : Co. of Biologists
Pages: - Volume / Issue: 25 (9) Sequence Number: - Start / End Page: 837 - 846 Identifier: ISSN: 0265-9247
CoNE: https://pure.mpg.de/cone/journals/resource/954925499109