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
Collections
Source
Angewandte Chemie International Edition
Type
Journal article
Book Title
Entity type
Access Statement
License Rights
Restricted until
2037-12-31