Title data
Romero-Romero, Sergio ; Kordes, Sina ; Michel, Florian ; Höcker, Birte:
Evolution, folding, and design of TIM barrels and related proteins.
In: Current Opinion in Structural Biology.
Vol. 68
(2021)
.
- pp. 94-104.
ISSN 0959-440X
DOI: https://doi.org/10.1016/j.sbi.2020.12.007
Project information
Project title: |
Project's official title Project's id ERC Consolidator Grant "Protein Lego" 647548 Volkswagenstiftung Grant 94747 Humboldt-Bayer Research Fellowship for Postdoctoral Researchers No information |
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Project financing: |
VolkswagenStiftung |
Abstract in another language
Proteins are chief actors in life that perform a myriad of exquisite functions. This diversity has been enabled through the evolution and diversification of protein folds. Analysis of sequences and structures strongly suggest that numerous protein pieces have been reused as building blocks and propagated to many modern folds. This information can be traced to understand how the protein world has diversified. In this review, we discuss the latest advances in the analysis of protein evolutionary units, and we use as a model system one of the most abundant and versatile topologies, the TIM-barrel fold, to highlight the existing common principles that interconnect protein evolution, structure, folding, function, and design.
Further data
Item Type: | Article in a journal |
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Refereed: | Yes |
Institutions of the University: | Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry > Chair Biochemistry - Univ.-Prof. Dr. Birte Höcker Faculties Faculties > Faculty of Biology, Chemistry and Earth Sciences Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry |
Result of work at the UBT: | Yes |
DDC Subjects: | 500 Science > 500 Natural sciences 500 Science > 570 Life sciences, biology |
Date Deposited: | 26 Jan 2021 07:47 |
Last Modified: | 27 Oct 2022 10:43 |
URI: | https://eref.uni-bayreuth.de/id/eprint/62397 |