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

doi:10.1002/cbic.201800350

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^*

^*Corresponding author for this work

5 Citations (Scopus)

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.

Original language	English
Journal	ChemBioChem
Volume	19
Issue number	20
Pages (from-to)	2136-2145
ISSN	1439-4227
DOIs	https://doi.org/10.1002/cbic.201800350
Publication status	Published - 18 Oct 2018

Keywords

amide-to-ester mutations
hydrogen bonds
protein backbone
proteins
structure and function

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10.1002/cbic.201800350

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title = "Probing Backbone Hydrogen Bonds in Proteins by Amide-to-Ester Mutations",

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.",

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T1 - Probing Backbone Hydrogen Bonds in Proteins by Amide-to-Ester Mutations

AU - Sereikaitė, Vita

AU - Jensen, Thomas M.T.

AU - Bartling, Christian R.O.

AU - Jemth, Per

AU - Pless, Stephan A.

AU - Strømgaard, Kristian

PY - 2018/10/18

Y1 - 2018/10/18

N2 - 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.

AB - 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.

KW - amide-to-ester mutations

KW - hydrogen bonds

KW - protein backbone

KW - proteins

KW - structure and function

U2 - 10.1002/cbic.201800350

DO - 10.1002/cbic.201800350

M3 - Review

C2 - 30073762

AN - SCOPUS:85054174294

SN - 1439-4227

VL - 19

SP - 2136

EP - 2145

JO - ChemBioChem

JF - ChemBioChem

IS - 20

ER -

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

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Keywords

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