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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

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

Zadorozhnyi Roman R Sarkar Sucharita S Quinn Caitlin M CM Zadrozny Kaneil K KK Ganser-Pornillos Barbie K BK Pornillos Owen O Gronenborn Angela M AM Polenova Tatyana T

Frontiers in molecular biosciences 20211210

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 <sup>1</sup>H detection with selective magnetization inversion tec ...[more]

PMID: 34957215

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