1H, 13C, 15N backbone resonance assignment of Escherichia coli adenylate kinase
Author:
Funder
National Institutes of Health
National Science Foundation
Publisher
Springer Science and Business Media LLC
Subject
Biochemistry,Structural Biology
Link
https://link.springer.com/content/pdf/10.1007/s12104-023-10147-1.pdf
Reference21 articles.
1. Ådén J, Verma A, Schug A, Wolf-Watz M (2012) Modulation of a pre-existing conformational equilibrium tunes adenylate kinase activity. J Am Chem Soc 134(40):16562–16570. https://doi.org/10.1021/ja3032482
2. Brom JA, Petrikis RG, Pielak GJ (2023) How sugars protect dry protein structure. Biochemistry 62(5):1044–1052. https://doi.org/10.1021/acs.biochem.2c00692
3. Burlacu-Miron S, Gilles A-M, Popescu A, BaÃrzu O, Craescu CT (1999a) Multinuclear magnetic resonance studies of Escherichia coli adenylate kinase in free and bound forms: resonance assignment, secondary structure and ligand binding. Eur J Biochem 264:765–774. https://doi.org/10.1046/j.1432-1327.1999.00633.x
4. Burlacu-Miron S, Perrier V, Gilles AM, Mispelter J, Bârzu O, Craescu CT (1999b) Letter to the editor: 1H, 13 C and 15 N backbone resonance assignment of Escherichia coli adenylate kinase, a 23.6 kDa protein. J Biomol NMR 13(1):93–94
5. Crilly CJ, Brom JA, Kowalewski ME, Piszkiewicz S, Pielak GJ (2021a) Dried protein structure revealed at the residue level by liquid-observed vapor exchange NMR. Biochemistry 60(2):152–159. https://doi.org/10.1021/acs.biochem.0c00863
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