ArticleThe journal of physical chemistry letters2010
NMR Determination of Protein pK(a) Values in the Solid State.
Article in The journal of physical chemistry letters, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Intermolecular β-sheet Formation Guides the Interaction between Ubiquitin-like Modifier FAT10 and Adapter Protein NUB1L.Journal of the American Chemical Society · 2026Article
- PKAD-R: curated, redesigned and expanded database of experimental pKa values in proteins.Journal of computational biophysics and chemistry · 2025Article
- In Situ Light-driven pH Modulation for NMR Studies.Angewandte Chemie (International ed. in English) · 2025Article
- Polar Networks Mediate Ion Conduction of the SARS-CoV-2 Envelope Protein.Journal of the American Chemical Society · 2025Article
- Protonation State of an Important Histidine from High Resolution Structures of Lytic Polysaccharide Monooxygenases.Biomolecules · 2022Article
- The molecular pH-response mechanism of the plant light-stress sensor PsbS.Nature communications · 2021Article
- 3D Interaction Homology: Computational Titration of Aspartic Acid, Glutamic Acid and Histidine Can Create pH-Tunable Hydropathic Environment Maps.Frontiers in molecular biosciences · 2021Article
- Deuterium-Enhanced Raman Spectroscopy for Histidine pKBiophysical journal · 2020Article
- Site-specific resolution of anionic residues in proteins using solid-state NMR spectroscopy.Journal of biomolecular NMR · 2020Article
- Rapid automated determination of chemical shift anisotropy values in the carbonyl and carboxyl groups of fd-y21m bacteriophage using solid state NMR.Journal of biomolecular NMR · 2018Article
- On the use of ultracentrifugal devices for routine sample preparation in biomolecular magic-angle-spinning NMR.Journal of biomolecular NMR · 2017Article
- Site-Specific Internal Motions in GB1 Protein Microcrystals Revealed by 3D ²H-¹³C-¹³C Solid-State NMR Spectroscopy.Journal of the American Chemical Society · 2016Article
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Authors and funding
4 authors.
Funding
Abstract
Charged residues play an important role in defining key mechanistic features in many biomolecules. Determining the pK(a) values of large, membrane or fibrillar proteins can be challenging with traditional methods. In this study we show how solid-state NMR is used to monitor chemical shift changes during a pH titration for the small soluble β1 immunoglobulin binding domain of protein G. The chemical shifts of all the amino acids with charged side-chains throughout the uniformly-(13)C,(15)N-labeled protein were monitored over several samples varying in pH; pK(a) values were determined from these shifts for E27, D36, and E42, and the bounds for the pK(a) of other acidic side-chain resonances were determined. Additionally, this study shows how the calculated pK(a) values give insights into the crystal packing of the protein.
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Registered trials
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