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Evolution, folding, and design of TIM barrels and related proteins

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
Protein Lego - Protein design from sub-domain sized fragments
647548

Project financing: Alexander von Humboldt-Stiftung
VolkswagenStiftung
European Research Council

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
Refereed: Yes
Institutions of the University: 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 I - Proteinbiochemie der Signaltransduktion
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry III - Protein Design > Chair Biochemistry III - Protein Design - Univ.-Prof. Dr. Birte Höcker
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry III - Protein Design
Research Institutions > EU Research Projects > Protein Lego - Protein Design from Sub-domain Sized Fragments
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: 10 Sep 2025 12:02
URI: https://eref.uni-bayreuth.de/id/eprint/62397