Determination of Histidine Protonation States in Proteins by Fast Magic Angle Spinning NMR.

ABSTRACT: Histidine residues play important structural and functional roles in proteins, such as serving as metal-binding ligands, mediating enzyme catalysis, and modulating proton channel activity. Many of these activities are modulated by the ionization state of the imidazole ring. Here we present a fast MAS NMR approach for the determination of protonation and tautomeric states of His at frequencies of 40-62 kHz. The experiments combine ¹H detection with selective magnetization inversion techniques and transferred echo double resonance (TEDOR)-based filters, in 2D heteronuclear correlation experiments. We illustrate this approach using microcrystalline assemblies of HIV-1 CA_CTD-SP1 protein.

SUBMITTER: Zadorozhnyi R 

PROVIDER: S-EPMC8703106 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature