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 af dette arbejde

5 Citationer (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.

Originalsprog	Engelsk
Tidsskrift	ChemBioChem
Vol/bind	19
Udgave nummer	20
Sider (fra-til)	2136-2145
ISSN	1439-4227
DOI	https://doi.org/10.1002/cbic.201800350
Status	Udgivet - 18 okt. 2018

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10.1002/cbic.201800350

Citationsformater

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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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author = "Vita Sereikaitė and Jensen, {Thomas M.T.} and Bartling, {Christian R.O.} and Per Jemth and Pless, {Stephan A.} and Kristian Str{\o}mgaard",

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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

Abstract

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