NMR “Crystallography” for Uniformly (13C, 15N)‐Labeled Oriented Membrane Proteins

In oriented‐sample (OS) solid‐state NMR of membrane proteins, the angular‐dependent dipolar couplings and chemical shifts provide a direct input for structure calculations. However, so far only 1H–15N dipolar couplings and 15N chemical shifts have been routinely assessed in oriented 15N‐labeled samp...

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Veröffentlicht in:	Angewandte Chemie International Edition 2020-02, Vol.59 (9), p.3554-3557
Hauptverfasser:	Awosanya, Emmanuel O., Lapin, Joel, Nevzorov, Alexander A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Carbon Isotopes - chemistry Coat protein Constraints Couplings Crystallography dipolar couplings Inovirus - metabolism Isotope Labeling Lipid Bilayers - chemistry Lipid Bilayers - metabolism Membrane proteins Membrane Proteins - chemistry Membranes Nitrogen isotopes Nitrogen Isotopes - chemistry NMR Nuclear magnetic resonance Nuclear Magnetic Resonance, Biomolecular Organic chemistry oriented samples Peptides Protein structure Proteins structure determination Topology Viral Proteins - chemistry
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