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Complete assignment of heteronuclear protein resonances by protonless NMR spectroscopy
- Source :
- Angewandte Chemie International Edition, Angewandte Chemie International Edition, Wiley-VCH Verlag, 2005, 44 (20), pp.3089-3092. ⟨10.1002/anie.200461794⟩, Angewandte Chemie International Edition, 2005, 44 (20), pp.3089-3092. ⟨10.1002/anie.200461794⟩
- Publication Year :
- 2005
-
Abstract
- Keywords: carbon NMR spectroscopy ; NMR spectroscopy ; protein structures ; proteins ; spin-state selection Reference EPFL-ARTICLE-204420doi:10.1002/anie.200461794View record in Web of Science Record created on 2015-01-08, modified on 2017-12-03
- Subjects :
- Carbon-13 NMR satellite
Nuclear magnetic resonance spectroscopy of nucleic acids
Fluorine-19 NMR
010402 general chemistry
01 natural sciences
Catalysis
03 medical and health sciences
NMR spectroscopy
Nuclear magnetic resonance
[CHIM]Chemical Sciences
Transverse relaxation-optimized spectroscopy
spin-state selection
Nuclear Magnetic Resonance, Biomolecular
ComputingMilieux_MISCELLANEOUS
030304 developmental biology
0303 health sciences
Carbon Isotopes
010405 organic chemistry
Chemistry
Proteins
General Medicine
General Chemistry
Nuclear magnetic resonance spectroscopy
Carbon-13 NMR
0104 chemical sciences
Crystallography
carbon NMR spectroscopy
protein structures
Protons
Two-dimensional nuclear magnetic resonance spectroscopy
Heteronuclear single quantum coherence spectroscopy
Subjects
Details
- ISSN :
- 14337851 and 15213773
- Volume :
- 44
- Issue :
- 20
- Database :
- OpenAIRE
- Journal :
- Angewandte Chemie (International ed. in English)
- Accession number :
- edsair.doi.dedup.....16204446b0162be5f02f347c9eaec7a9
- Full Text :
- https://doi.org/10.1002/anie.200461794⟩