Proton-detected solid-state NMR spectroscopy of fibrillar and membrane proteins

Rasmus Linser; Muralidhar Dasari; Matthias Hiller; Victoria Higman; Uwe Fink; Juan Miguel Lopez Del Amo; Stefan Markovic; Liselotte Handel; Brigitte Kessler; Peter Schmieder; Dieter Oesterhelt; Hartmut Oschkinat; Bernd Reif

doi:10.1002/anie.201008244

Proton-detected solid-state NMR spectroscopy of fibrillar and membrane proteins

Rasmus Linser
, Muralidhar Dasari
, Matthias Hiller
, Victoria Higman
, Uwe Fink
, Juan Miguel Lopez Del Amo
, Stefan Markovic
, Liselotte Handel
, Brigitte Kessler
, Peter Schmieder
, Dieter Oesterhelt
, Hartmut Oschkinat
, Bernd Reif

Associate Professorship of Solid-State NMR spectroscopy

Leibniz-Institut für Molekulare Pharmakologie
University of New South Wales
Technical University of Munich
Helmholtz Zentrum München German Research Center for Environmental Health
University of Oxford Medical Sciences Division
Max Planck Institute of Biochemistry

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

171 Scopus citations

Abstract

Structural characterization of insoluble proteins often relies on solid-state NMR spectroscopy. Perdeuteration and partial back-substitution of exchangeable protons, as proposed for crystalline model proteins, is now shown to lead to beneficial proton spectra for heterogeneous systems, such as fibrils formed by the Alzheimer's disease β-amyloid peptide Aβ40, the lipid reconstituted β-barrel membrane protein OmpG, and the α-helical membrane protein bacteriorhodopsin.

Original language	English
Pages (from-to)	4508-4512
Number of pages	5
Journal	Angewandte Chemie International Edition in English
Volume	50
Issue number	19
DOIs	https://doi.org/10.1002/anie.201008244
State	Published - 2 May 2011

Keywords

amyloid fibrils
lipid membrane
membrane proteins
outer membrane protein G
solid-state NMR spectroscopy

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10.1002/anie.201008244

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Linser, R., Dasari, M., Hiller, M., Higman, V., Fink, U., Lopez Del Amo, J. M., Markovic, S., Handel, L., Kessler, B., Schmieder, P., Oesterhelt, D., Oschkinat, H., & Reif, B. (2011). Proton-detected solid-state NMR spectroscopy of fibrillar and membrane proteins. Angewandte Chemie International Edition in English, 50(19), 4508-4512. https://doi.org/10.1002/anie.201008244

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title = "Proton-detected solid-state NMR spectroscopy of fibrillar and membrane proteins",

abstract = "Structural characterization of insoluble proteins often relies on solid-state NMR spectroscopy. Perdeuteration and partial back-substitution of exchangeable protons, as proposed for crystalline model proteins, is now shown to lead to beneficial proton spectra for heterogeneous systems, such as fibrils formed by the Alzheimer's disease β-amyloid peptide Aβ40, the lipid reconstituted β-barrel membrane protein OmpG, and the α-helical membrane protein bacteriorhodopsin.",

keywords = "amyloid fibrils, lipid membrane, membrane proteins, outer membrane protein G, solid-state NMR spectroscopy",

author = "Rasmus Linser and Muralidhar Dasari and Matthias Hiller and Victoria Higman and Uwe Fink and \{Lopez Del Amo\}, \{Juan Miguel\} and Stefan Markovic and Liselotte Handel and Brigitte Kessler and Peter Schmieder and Dieter Oesterhelt and Hartmut Oschkinat and Bernd Reif",

year = "2011",

month = may,

day = "2",

doi = "10.1002/anie.201008244",

language = "English",

volume = "50",

pages = "4508--4512",

journal = "Angewandte Chemie International Edition in English",

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Linser, R, Dasari, M, Hiller, M, Higman, V, Fink, U, Lopez Del Amo, JM, Markovic, S, Handel, L, Kessler, B, Schmieder, P, Oesterhelt, D, Oschkinat, H & Reif, B 2011, 'Proton-detected solid-state NMR spectroscopy of fibrillar and membrane proteins', Angewandte Chemie International Edition in English, vol. 50, no. 19, pp. 4508-4512. https://doi.org/10.1002/anie.201008244

TY - JOUR

T1 - Proton-detected solid-state NMR spectroscopy of fibrillar and membrane proteins

AU - Linser, Rasmus

AU - Dasari, Muralidhar

AU - Hiller, Matthias

AU - Higman, Victoria

AU - Fink, Uwe

AU - Lopez Del Amo, Juan Miguel

AU - Markovic, Stefan

AU - Handel, Liselotte

AU - Kessler, Brigitte

AU - Schmieder, Peter

AU - Oesterhelt, Dieter

AU - Oschkinat, Hartmut

AU - Reif, Bernd

PY - 2011/5/2

Y1 - 2011/5/2

N2 - Structural characterization of insoluble proteins often relies on solid-state NMR spectroscopy. Perdeuteration and partial back-substitution of exchangeable protons, as proposed for crystalline model proteins, is now shown to lead to beneficial proton spectra for heterogeneous systems, such as fibrils formed by the Alzheimer's disease β-amyloid peptide Aβ40, the lipid reconstituted β-barrel membrane protein OmpG, and the α-helical membrane protein bacteriorhodopsin.

AB - Structural characterization of insoluble proteins often relies on solid-state NMR spectroscopy. Perdeuteration and partial back-substitution of exchangeable protons, as proposed for crystalline model proteins, is now shown to lead to beneficial proton spectra for heterogeneous systems, such as fibrils formed by the Alzheimer's disease β-amyloid peptide Aβ40, the lipid reconstituted β-barrel membrane protein OmpG, and the α-helical membrane protein bacteriorhodopsin.

KW - amyloid fibrils

KW - lipid membrane

KW - membrane proteins

KW - outer membrane protein G

KW - solid-state NMR spectroscopy

UR - https://www.scopus.com/pages/publications/79955487946

U2 - 10.1002/anie.201008244

DO - 10.1002/anie.201008244

M3 - Article

C2 - 21495136

AN - SCOPUS:79955487946

SN - 1433-7851

VL - 50

SP - 4508

EP - 4512

JO - Angewandte Chemie International Edition in English

JF - Angewandte Chemie International Edition in English

IS - 19

ER -

Proton-detected solid-state NMR spectroscopy of fibrillar and membrane proteins

Abstract

Keywords

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