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  Simple mechanisms for the evolution of protein complexity

Pillai, A. S., Hochberg, G. K. A., & Thornton, J. W. (2022). Simple mechanisms for the evolution of protein complexity. Protein Science, 31(11): e4449. doi:10.1002/pro.4449.

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Genre: Journal Article
Alternative Title : PROTEIN SCIENCE

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https://doi.org/10.1002/pro.4449 (Publisher version)
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 Creators:
Pillai, Arvind S.1, Author
Hochberg, Georg K. A.2, 3, 4, Author                 
Thornton, Joseph W.1, Author
Affiliations:
1external, ou_persistent22              
2Max Planck Research Group Evolutionary Biochemistry, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266300              
3Center for Synthetic Microbiology, Philipps-Universität Marburg, ou_persistent22              
4Department of Chemistry, Philipps-Universität Marburg, ou_persistent22              

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 Abstract: Proteins are tiny models of biological complexity: specific interactions among their many amino acids cause proteins to fold into elaborate structures, assemble with other proteins into higher-order complexes, and change their functions and structures upon binding other molecules. These complex features are classically thought to evolve via long and gradual trajectories driven by persistent natural selection. But a growing body of evidence from biochemistry, protein engineering, and molecular evolution shows that naturally occurring proteins often exist at or near the genetic edge of multimerization, allostery, and even new folds, so just one or a few mutations can trigger acquisition of these properties. These sudden transitions can occur because many of the physical properties that underlie these features are present in simpler proteins as fortuitous by-products of their architecture. Moreover, complex features of proteins can be encoded by huge arrays of sequences, so they are accessible from many different starting points via many possible paths. Because the bridges to these features are both short and numerous, random chance can join selection as a key factor in explaining the evolution of molecular complexity.

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 Dates: 2022
 Publication Status: Issued
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 Identifiers: DOI: 10.1002/pro.4449
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Title: Protein Science
Source Genre: Journal
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Publ. Info: Hoboken, New Jersey, Vereinigte Staaten : Wiley
Pages: - Volume / Issue: 31 (11) Sequence Number: e4449 Start / End Page: - Identifier: ISSN: 0961-8368
CoNE: https://pure.mpg.de/cone/journals/resource/954925342760