Aromatic spectral editing techniques for magic-angle-spinning solid-state NMR spectroscopy of uniformly 13C-labeled proteins
The four aromatic amino acids in proteins, namely histidine, phenylalanine, tyrosine, and tryptophan, have strongly overlapping ¹³C chemical shift ranges between 100 and 160 ppm, and have so far been largely neglected in solid-state NMR determination of protein structures. Yet aromatic residues play...
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| Format: | Article |
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Elsevier
2018
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| Online Access: | http://hdl.handle.net/1721.1/113323 https://orcid.org/0000-0002-7272-6885 https://orcid.org/0000-0001-5255-5858 |