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Probing Backbone Hydrogen Bonds in Proteins by Amide-to-Ester Mutations
Univ Copenhagen, Dept Drug Design & Pharmacol, Ctr Biopharmaceut, Univ Pk 2, DK-2200 Copenhagen, Denmark.
Univ Copenhagen, Dept Drug Design & Pharmacol, Ctr Biopharmaceut, Univ Pk 2, DK-2200 Copenhagen, Denmark.
Univ Copenhagen, Dept Drug Design & Pharmacol, Ctr Biopharmaceut, Univ Pk 2, DK-2200 Copenhagen, Denmark.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
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2018 (English)In: ChemBioChem (Print), ISSN 1439-4227, E-ISSN 1439-7633, Vol. 19, no 20, p. 2136-2145Article, review/survey (Refereed) Published
Abstract [en]

All proteins contain characteristic backbones formed of consecutive amide bonds, which can engage in hydrogen bonds. However, the importance of these is not easily addressed by conventional technologies that only allow for side-chain substitutions. By contrast, technologies such as nonsense suppression mutagenesis and protein ligation allow for manipulation of the protein backbone. In particular, replacing the backbone amide groups with ester groups, that is, amide-to-ester mutations, is a powerful tool to examine backbone-mediated hydrogen bonds. In this minireview, we showcase examples of how amide-to-ester mutations can be used to uncover pivotal roles of backbone-mediated hydrogen bonds in protein recognition, folding, function, and structure.

Place, publisher, year, edition, pages
Wiley-VCH Verlagsgesellschaft, 2018. Vol. 19, no 20, p. 2136-2145
Keywords [en]
amide-to-ester mutations, hydrogen bonds, protein backbone, proteins, structure and function
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-369617DOI: 10.1002/cbic.201800350ISI: 000447635300002PubMedID: 30073762OAI: oai:DiVA.org:uu-369617DiVA, id: diva2:1271322
Funder
Swedish Research CouncilAvailable from: 2018-12-17 Created: 2018-12-17 Last updated: 2018-12-17Bibliographically approved

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Jemth, Per

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