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Identification and Analysis of Natural Building Blocks for Evolution-Guided Fragment-Based Protein Design

Title data

Ferruz, Noelia ; Lobos, Francisco ; Lemm, Dominik ; Toledo-Patiño, Saacnicteh ; Farías-Rico, José Arcadio ; Schmidt, Steffen ; Höcker, Birte:
Identification and Analysis of Natural Building Blocks for Evolution-Guided Fragment-Based Protein Design.
In: Journal of Molecular Biology. Vol. 432 (12 June 2020) Issue 13 . - pp. 3898-3914.
ISSN 0022-2836
DOI: https://doi.org/10.1016/j.jmb.2020.04.013

Project information

Project title:
Project's official titleProject's id
DFG GrantHO 4022/1-2
VolkwagenStiftung Grant94747
ERC Consolidator Grant "Protein Lego"647548

Project financing: Deutsche Forschungsgemeinschaft

Abstract in another language

Natural evolution has generated an impressively diverse protein universe via duplication and recombination from a set of protein fragments that served as building blocks. The application of these concepts to the design of new proteins using subdomain-sized fragments from different folds has proven to be experimentally successful. To better understand how evolution has shaped our protein universe, we performed an all-against-all comparison of protein domains representing all naturally existing folds and identified conserved homologous protein fragments. Overall, we found more than 1000 protein fragments of various lengths among different folds through similarity network analysis. These fragments are present in very different protein environments and represent versatile building blocks for protein design. These data are available in our web server called F(old P)uzzle (fuzzle.uni-bayreuth.de), which allows to individually filter the dataset and create customized networks for folds of interest. We believe that our results serve as an invaluable resource for structural and evolutionary biologists and as raw material for the design of custom-made proteins.

Further data

Item Type: Article in a journal
Refereed: Yes
Keywords: Evolution; Protein design; Protein fragments; Protein recombination
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry > Chair Biochemistry - Univ.-Prof. Dr. Birte Höcker
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 07:36
Last Modified: 26 Jan 2021 07:36
URI: https://eref.uni-bayreuth.de/id/eprint/62393