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Evolutionary protein stabilization in comparison with computational design

Title data

Wunderlich, Michael ; Martin, Andreas ; Staab, Claudia A. ; Schmid, Franz X.:
Evolutionary protein stabilization in comparison with computational design.
In: Journal of Molecular Biology. Vol. 351 (2 September 2005) Issue 5 . - pp. 1160-1168.
ISSN 0022-2836
DOI: https://doi.org/10.1016/j.jmb.2005.06.059

Official URL: Volltext

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Abstract in another language

Two major strategies are currently used for stabilizing proteins: in vitro evolution and computational design. Here, we used gene libraries of the beta1 domain of the streptococcal protein G (Gbeta1) and Proside, an in vitro selection method, to identify stabilized variants of this protein. In the Gbeta1 libraries, the codons for the four boundary positions 16, 18, 25, and 29 were randomized. Many Gbeta1 variants with strongly increased thermal stabilities were found in 11 selections performed with five independent libraries. Previously, Mayo and co-workers used computational design to stabilize Gbeta1 by sequence optimization at the same positions. Their best variant ranked third within the panel of the selected variants. None of the ten computed sequences was found in the Proside selections, because several computed residues for positions 18 and 29 were not optimal for stability.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 16051264
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors > Professorship Biochemistry - Univ.-Prof. Dr. Franz Xaver Schmid
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 > Professorship Biochemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 24 Apr 2015 08:26
Last Modified: 08 Jun 2015 13:11
URI: https://eref.uni-bayreuth.de/id/eprint/10646