Complete Assignment of Aromatic 1H Nuclear Magnetic Resonances of the Tyrosine Residues of Hen Lysozyme
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1978.tb12726.x/fullpdf
Reference22 articles.
1. Nuclear magnetic resonance studies on the structure of lysozyme in solution
2. Study of the Tryptophan Residues of Lysozyme Using 1H Nuclear Magnetic Resonance
3. 3. K. Wuthrich, G. Wagner, R. Richarz, A. Marco, R. A. Dwek, I. D. Campbell, R. E. Richards, and R. J. P. Williams (1977 ) inNMR in Biology () pp.51 -62 . Academic Press, New York.
4. Studies of individual carbon sites of hen egg white lysozyme by natural abundance carbon 13 nuclear magnetic resonance spectroscopy. Assignment of the nonprotonated aromatic carbon resonances to specific residues in the sequence.
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