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Comparison of different modes of two-dimensional reverse-correlation NMR for the study of proteins

โœ Scribed by Ad Bax; Mitsuhiko Ikura; Lewis E Kay; Dennis A Torchia; Rolf Tschudin

Publisher
Elsevier Science
Year
1990
Weight
1012 KB
Volume
86
Category
Article
ISSN
0022-2364

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As aromatic residues very often are part of the hydrophobic essential for an accurate and precise structure determination. core of proteins, the unambiguous assignment of the aromatic Therefore, methods for the unambiguous assignment of aroproton resonances is essential for an accurate and precise s