Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 51, Issue -, Pages 106-115Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2018.02.007
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Funding
- Feder Funds from the Spanish Ministry of Economy and Competitiveness [B102015-66426-R]
- Human Frontier Science Program [RGP0041/2017]
- NSF-MCB [1715591]
- RCS
- Gordon & Betty Moore Foundation
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1715591] Funding Source: National Science Foundation
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Approximations to the sequences of ancestral proteins can be derived from the sequences of their modern descendants. Proteins encoded by such reconstructed sequences can be prepared in the laboratory and subjected to experimental scrutiny. These 'resurrected' ancestral proteins often display remarkable properties, reflecting ancestral adaptations to intra-cellular and extra-cellular environments that differed from the environments hosting modern/extant proteins. Recent experimental and computational work has specifically discussed high stability, substrate and catalytic promiscuity, conformational flexibility/diversity and altered patterns of interaction with other sub-cellular components. In this review, we discuss these remarkable properties as well as recent attempts to explore their biotechnological and protein engineering potential.
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