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Probing Backbone Hydrogen Bonds in Proteins by Amide‐to‐Ester Mutations
Author(s) -
Sereikaitė Vita,
Jensen Thomas M. T.,
Bartling Christian R. O.,
Jemth Per,
Pless Stephan A.,
Strømgaard Kristian
Publication year - 2018
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201800350
Subject(s) - hydrogen bond , amide , chemistry , side chain , mutagenesis , peptide bond , folding (dsp implementation) , stereochemistry , combinatorial chemistry , mutation , amino acid , biochemistry , molecule , organic chemistry , polymer , gene , electrical engineering , engineering
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.