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Backbone Assignment of Fully Protonated Solid Proteins by1H Detection and Ultrafast Magic-Angle-Spinning NMR Spectroscopy
- Source :
- Angewandte Chemie International Edition, Angewandte Chemie International Edition, Wiley-VCH Verlag, 2012, 51 (43), pp.10756-10759. ⟨10.1002/anie.201203124⟩, Angewandte Chemie International Edition, 2012, 51 (43), pp.10756-10759. ⟨10.1002/anie.201203124⟩
- Publication Year :
- 2012
- Publisher :
- Wiley, 2012.
-
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. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
- Subjects :
- STRUCTURAL BASIS
magic-angle spinning
TERMINAL DOMAIN
Protonation
DNA polymerase
010402 general chemistry
01 natural sciences
Catalysis
NMR spectroscopy
Protein structure
Magic angle spinning
Transverse relaxation-optimized spectroscopy
Spectroscopy
Nuclear Magnetic Resonance, Biomolecular
ComputingMilieux_MISCELLANEOUS
DNA Polymerase III
Carbon Isotopes
Nitrogen Isotopes
010405 organic chemistry
Chemistry
scalar transfers
Proteins
PEPTIDES
General Medicine
General Chemistry
Nuclear magnetic resonance spectroscopy
Deuterium
0104 chemical sciences
[CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry
Crystallography
MAS
RESOLUTION
STATE NMR
protein structures
Proton NMR
Protons
Hydrogen
Subjects
Details
- ISSN :
- 14337851 and 15213773
- Volume :
- 51
- Database :
- OpenAIRE
- Journal :
- Angewandte Chemie International Edition
- Accession number :
- edsair.doi.dedup.....7cb4fae455c45e6f28f21a7c1ae5762f
- Full Text :
- https://doi.org/10.1002/anie.201203124