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Probing Backbone Hydrogen Bonds in Proteins by Amide-to-Ester Mutations

Probing Backbone Hydrogen Bonds in Proteins by Amide-to-Ester Mutations

Vita Sereikaitė, Thomas M T Jensen, Christian R O Bartling, Per Jemth, Stephan A Pless, Kristian Strømgaard

Chembiochem. 2018 Oct 18;19(20):2136-2145.

PMID: 30073762

Abstract:

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP104809292	Nle-Arg-Phe amide		104809-29-2	Price
AP155206001	17-Phenyl-tri-norprostaglandin F2α-ethyl amide		155206-00-1	Price

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