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

Research output: Contribution to journal › Review › Research › peer-review

Standard

Probing Backbone Hydrogen Bonds in Proteins by Amide-to-Ester Mutations. / Sereikaitė, Vita; Jensen, Thomas M.T.; Bartling, Christian R.O.; Jemth, Per; Pless, Stephan A.; Strømgaard, Kristian.

In: ChemBioChem, Vol. 19, No. 20, 18.10.2018, p. 2136-2145.

Research output: Contribution to journal › Review › Research › peer-review

Harvard

Sereikaitė, V, Jensen, TMT, Bartling, CRO, Jemth, P, Pless, SA & Strømgaard, K 2018, 'Probing Backbone Hydrogen Bonds in Proteins by Amide-to-Ester Mutations', ChemBioChem, vol. 19, no. 20, pp. 2136-2145. https://doi.org/10.1002/cbic.201800350

APA

Sereikaitė, V., Jensen, T. M. T., Bartling, C. R. O., Jemth, P., Pless, S. A., & Strømgaard, K. (2018). Probing Backbone Hydrogen Bonds in Proteins by Amide-to-Ester Mutations. ChemBioChem, 19(20), 2136-2145. https://doi.org/10.1002/cbic.201800350

Vancouver

Sereikaitė V, Jensen TMT, Bartling CRO, Jemth P, Pless SA, Strømgaard K. Probing Backbone Hydrogen Bonds in Proteins by Amide-to-Ester Mutations. ChemBioChem. 2018 Oct 18;19(20):2136-2145. https://doi.org/10.1002/cbic.201800350

Author

Sereikaitė, Vita ; Jensen, Thomas M.T. ; Bartling, Christian R.O. ; Jemth, Per ; Pless, Stephan A. ; Strømgaard, Kristian. / Probing Backbone Hydrogen Bonds in Proteins by Amide-to-Ester Mutations. In: ChemBioChem. 2018 ; Vol. 19, No. 20. pp. 2136-2145.

Bibtex

@article{dad735a6d6c044e8a831c64319d17811,
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.",
keywords = "amide-to-ester mutations, hydrogen bonds, protein backbone, proteins, structure and function",
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",
year = "2018",
month = oct,
day = "18",
doi = "10.1002/cbic.201800350",
language = "English",
volume = "19",
pages = "2136--2145",
journal = "ChemBioChem",
issn = "1439-4227",
publisher = "Wiley - V C H Verlag GmbH & Co. KGaA",
number = "20",

}

RIS

TY - JOUR

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

VL - 19

SP - 2136

EP - 2145

JO - ChemBioChem

JF - ChemBioChem

SN - 1439-4227

IS - 20

ER -

ID: 204112661