Probing the conformational diversity of cancer-associated mutations in p53 with ion-mobility mass spectrometry

Ewa Jurneczko; Faye Cruickshank; Massimiliano Porrini; David J. Clarke; Iain D G Campuzano; Michael Morris; Penka V. Nikolova; Perdita E. Barran

doi:10.1002/anie.201210015

Probing the conformational diversity of cancer-associated mutations in p53 with ion-mobility mass spectrometry

Ewa Jurneczko, Faye Cruickshank, Massimiliano Porrini, David J. Clarke, Iain D G Campuzano, Michael Morris, Penka V. Nikolova, Perdita E. Barran

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

Abstract

Conformational flexibility: The DNA-binding domain of tumor suppressor protein p53 (see picture) is characterized by using ion-mobility mass spectrometry. Wild-type p53 and common single-point carcinogenic mutations exhibit diverse conformational states upon transfer into a solvent-free environment of the mass spectrometer. DNA-binding properties of wild-type p53 and an engineered second-site suppressor mutation H115N were also investigated. Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Original language	English
Pages (from-to)	4370-4374
Number of pages	4
Journal	Angewandte Chemie - International Edition
Volume	52
Issue number	16
DOIs	https://doi.org/10.1002/anie.201210015
Publication status	Published - 15 Apr 2013

Keywords

conformation analysis
DNA
mass spectrometry
p53 protein
protein structures

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1002/anie.201210015

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title = "Probing the conformational diversity of cancer-associated mutations in p53 with ion-mobility mass spectrometry",

abstract = "Conformational flexibility: The DNA-binding domain of tumor suppressor protein p53 (see picture) is characterized by using ion-mobility mass spectrometry. Wild-type p53 and common single-point carcinogenic mutations exhibit diverse conformational states upon transfer into a solvent-free environment of the mass spectrometer. DNA-binding properties of wild-type p53 and an engineered second-site suppressor mutation H115N were also investigated. Copyright {\textcopyright} 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.",

keywords = "conformation analysis, DNA, mass spectrometry, p53 protein, protein structures",

author = "Ewa Jurneczko and Faye Cruickshank and Massimiliano Porrini and Clarke, {David J.} and Campuzano, {Iain D G} and Michael Morris and Nikolova, {Penka V.} and Barran, {Perdita E.}",

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AU - Jurneczko, Ewa

AU - Cruickshank, Faye

AU - Porrini, Massimiliano

AU - Clarke, David J.

AU - Campuzano, Iain D G

AU - Morris, Michael

AU - Nikolova, Penka V.

AU - Barran, Perdita E.

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PY - 2013/4/15

Y1 - 2013/4/15

N2 - Conformational flexibility: The DNA-binding domain of tumor suppressor protein p53 (see picture) is characterized by using ion-mobility mass spectrometry. Wild-type p53 and common single-point carcinogenic mutations exhibit diverse conformational states upon transfer into a solvent-free environment of the mass spectrometer. DNA-binding properties of wild-type p53 and an engineered second-site suppressor mutation H115N were also investigated. Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

AB - Conformational flexibility: The DNA-binding domain of tumor suppressor protein p53 (see picture) is characterized by using ion-mobility mass spectrometry. Wild-type p53 and common single-point carcinogenic mutations exhibit diverse conformational states upon transfer into a solvent-free environment of the mass spectrometer. DNA-binding properties of wild-type p53 and an engineered second-site suppressor mutation H115N were also investigated. Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

KW - conformation analysis

KW - DNA

KW - mass spectrometry

KW - p53 protein

KW - protein structures

U2 - 10.1002/anie.201210015

DO - 10.1002/anie.201210015

M3 - Article

SN - 1433-7851

VL - 52

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EP - 4374

JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

IS - 16

ER -

Probing the conformational diversity of cancer-associated mutations in p53 with ion-mobility mass spectrometry

Abstract

Keywords

UN SDGs

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