Mass spectrometry assisted arginine side chains assignment of NMR resonances in natural abundance proteins
Author:
Funder
National Natural Science Foundation of China
Publisher
Springer Science and Business Media LLC
Subject
Spectroscopy,Biochemistry
Link
http://link.springer.com/content/pdf/10.1007/s10858-020-00302-4.pdf
Reference42 articles.
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3. Bartlett GJ, Porter CT, Borkakoti N, Thornton JM (2002) Analysis of catalytic residues in enzyme active sites. J Mol Biol 324:105–121
4. Berglund H, Baumann H, Knapp S, Ladenstein R, Haerd T (1995) Flexibility of an arginine side chain at a DNA-protein interface. J Am Chem Soc 117:12883–12884
5. Birdsall B, Polshakov VI, Feeney J (2000) NMR studies of ligand carboxylate group interactions with arginine residues in complexes of Lactobacillus casei dihydrofolate reductase with substrates and substrate analogues. Biochemistry 39:9819–9825
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