1 H, 13 C, 15 N backbone resonance assignment of Escherichia coli adenylate kinase.
Julia A BromSasiprapa SamsriRuta G PetrikisStuart ParnhamGary J PielakPublished in: Biomolecular NMR assignments (2023)
Adenylate kinase reversibly catalyzes the conversion of ATP plus AMP to two ADPs. This essential catalyst is present in every cell, and the Escherichia coli protein is often employed as a model enzyme. Our aim is to use the E. coli enzyme to understand dry protein structure and protection. Here, we report the expression, purification, steady-state assay, NMR conditions and 1 H, 13 C, 15 N backbone resonance NMR assignments of its C77S variant. These data will also help others utilize this prototypical enzyme.
Keyphrases
- escherichia coli
- protein kinase
- magnetic resonance
- energy transfer
- high resolution
- binding protein
- poor prognosis
- protein protein
- solid state
- tyrosine kinase
- klebsiella pneumoniae
- single cell
- amino acid
- biofilm formation
- electronic health record
- small molecule
- stem cells
- ionic liquid
- bone marrow
- big data
- gold nanoparticles
- mesenchymal stem cells
- multidrug resistant
- cystic fibrosis
- carbon dioxide
- data analysis
- pseudomonas aeruginosa
- quantum dots
- artificial intelligence