Backbone assignment of fully protonated solid proteins by 1H detection and ultrafast magic-angle-spinning NMR spectroscopy

Alessandro Marchetti; Stefan Jehle; Michele Felletti; Michael J. Knight; Yao Wang; Zhi Qiang Xu; Ah Young Park; Gottfried Otting; Anne Lesage; Lyndon Emsley; Nicholas E. Dixon; Guido Pintacuda

doi:10.1002/anie.201203124

Backbone assignment of fully protonated solid proteins by ¹H detection and ultrafast magic-angle-spinning NMR spectroscopy

Alessandro Marchetti, Stefan Jehle, Michele Felletti, Michael J. Knight, Yao Wang, Zhi Qiang Xu, Ah Young Park, Gottfried Otting, Anne Lesage, Lyndon Emsley, Nicholas E. Dixon, Guido Pintacuda^*

^*Corresponding author for this work

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

91 Citations (Scopus)

Abstract

Narrow ¹H NMR linewidths can be obtained for fully protonated protein samples in the solid state by using ultrafast magic-angle spinning (60 kHz). Medium-size microcrystalline and noncrystalline proteins can be analyzed without any need for deuteration of the protein sample. This approach provides assignments of the backbone ¹H, ¹⁵N, ¹³C ^α, and ¹³CO resonances and yields information about ¹H-¹H proximities.

Original language	English
Pages (from-to)	10756-10759
Number of pages	4
Journal	Angewandte Chemie - International Edition
Volume	51
Issue number	43
DOIs	https://doi.org/10.1002/anie.201203124
Publication status	Published - 22 Oct 2012

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Marchetti, A., Jehle, S., Felletti, M., Knight, M. J., Wang, Y., Xu, Z. Q., Park, A. Y., Otting, G., Lesage, A., Emsley, L., Dixon, N. E., & Pintacuda, G. (2012). Backbone assignment of fully protonated solid proteins by ¹H detection and ultrafast magic-angle-spinning NMR spectroscopy. Angewandte Chemie - International Edition, 51(43), 10756-10759. https://doi.org/10.1002/anie.201203124

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title = "Backbone assignment of fully protonated solid proteins by 1H detection and ultrafast magic-angle-spinning NMR spectroscopy",

abstract = "Narrow 1H NMR linewidths can be obtained for fully protonated protein samples in the solid state by using ultrafast magic-angle spinning (60 kHz). Medium-size microcrystalline and noncrystalline proteins can be analyzed without any need for deuteration of the protein sample. This approach provides assignments of the backbone 1H, 15N, 13C α, and 13CO resonances and yields information about 1H-1H proximities.",

keywords = "DNA polymerase, NMR spectroscopy, magic-angle spinning, protein structures, scalar transfers",

author = "Alessandro Marchetti and Stefan Jehle and Michele Felletti and Knight, {Michael J.} and Yao Wang and Xu, {Zhi Qiang} and Park, {Ah Young} and Gottfried Otting and Anne Lesage and Lyndon Emsley and Dixon, {Nicholas E.} and Guido Pintacuda",

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month = oct,

day = "22",

doi = "10.1002/anie.201203124",

language = "English",

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Marchetti, A, Jehle, S, Felletti, M, Knight, MJ, Wang, Y, Xu, ZQ, Park, AY, Otting, G, Lesage, A, Emsley, L, Dixon, NE & Pintacuda, G 2012, 'Backbone assignment of fully protonated solid proteins by ¹H detection and ultrafast magic-angle-spinning NMR spectroscopy', Angewandte Chemie - International Edition, vol. 51, no. 43, pp. 10756-10759. https://doi.org/10.1002/anie.201203124

TY - JOUR

T1 - Backbone assignment of fully protonated solid proteins by 1H detection and ultrafast magic-angle-spinning NMR spectroscopy

AU - Marchetti, Alessandro

AU - Jehle, Stefan

AU - Felletti, Michele

AU - Knight, Michael J.

AU - Wang, Yao

AU - Xu, Zhi Qiang

AU - Park, Ah Young

AU - Otting, Gottfried

AU - Lesage, Anne

AU - Emsley, Lyndon

AU - Dixon, Nicholas E.

AU - Pintacuda, Guido

PY - 2012/10/22

Y1 - 2012/10/22

N2 - Narrow 1H NMR linewidths can be obtained for fully protonated protein samples in the solid state by using ultrafast magic-angle spinning (60 kHz). Medium-size microcrystalline and noncrystalline proteins can be analyzed without any need for deuteration of the protein sample. This approach provides assignments of the backbone 1H, 15N, 13C α, and 13CO resonances and yields information about 1H-1H proximities.

AB - Narrow 1H NMR linewidths can be obtained for fully protonated protein samples in the solid state by using ultrafast magic-angle spinning (60 kHz). Medium-size microcrystalline and noncrystalline proteins can be analyzed without any need for deuteration of the protein sample. This approach provides assignments of the backbone 1H, 15N, 13C α, and 13CO resonances and yields information about 1H-1H proximities.

KW - DNA polymerase

KW - NMR spectroscopy

KW - magic-angle spinning

KW - protein structures

KW - scalar transfers

UR - http://www.scopus.com/inward/record.url?scp=84867548984&partnerID=8YFLogxK

U2 - 10.1002/anie.201203124

DO - 10.1002/anie.201203124

M3 - Article

SN - 1433-7851

VL - 51

SP - 10756

EP - 10759

JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

IS - 43

ER -

Backbone assignment of fully protonated solid proteins by ¹H detection and ultrafast magic-angle-spinning NMR spectroscopy

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