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

Date

2012

Authors

Marchetti, Alessandro
Jehle, Stefan
Felletti, Michele
Knight, Michael J.
Wang, Yao
Xu, Zhi-Qiang
Park, Ah Young
Lesage, Anne
Emsley, Lyndon
Dixon, Nicholas Edward

Journal Title

Journal ISSN

Volume Title

Publisher

Wiley-VCH Verlag GMBH

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.

Description

Keywords

Keywords: Deuterations; DNA polymerase; Magic-angle-spinning NMR; Noncrystalline proteins; Protein samples; Protein structures; Protonated; scalar transfers; Solid protein; Ultra-fast; Deuterium; Nuclear magnetic resonance spectroscopy; Proteins; Protonation; Magic DNA polymerase; magic-angle spinning; NMR spectroscopy; protein structures; scalar transfers

Citation

Source

Angewandte Chemie International Edition

Type

Journal article

Book Title

Entity type

Access Statement

License Rights

DOI

10.1002/anie.201203124

Restricted until

2037-12-31