ArticleFrontiers in molecular biosciences2020
Sedimentation Yields Long-Term Stable Protein Samples as Shown by Solid-State NMR.
Article in Frontiers in molecular biosciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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29 citing papers in PubMed, 46 citations in OpenAlex.
- Characterization of Full-Length Antibody Complexes Through HDX-Mass Spectrometry Coupled With NMR Spectroscopy: New Insight Into Avelumab/PD-L1 Interaction.Angewandte Chemie (International ed. in English) · 2026Article
- Spotlight on the Nucleotide: Solid-State NMR for the Investigation of ATP Hydrolysis in the ATPase SmsC.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- Co-sedimentation is the key to the structural investigation of wild-type FAT10.Journal of biomolecular NMR · 2026Article
- Structural and mechanistic insights into primer synthesis initiation by DNA primase.Nature communications · 2026Article
- Solid-state NMR of membrane peptides and proteins in the lipid cubic phase.Biophysical journal · 2025Article
- Probing Biomolecular Interactions with Paramagnetic Nuclear Magnetic Resonance Spectroscopy.Chembiochem : a European journal of chemical biology · 2025Review
- Sedimentation of large, soluble proteins up to 140 kDa forJournal of biomolecular NMR · 2024Article
- Initial Primer Synthesis of a DNA Primase Monitored by Real-Time NMR Spectroscopy.Journal of the American Chemical Society · 2024Article
- The assembly platform FimD is required to obtain the most stable quaternary structure of type 1 pili.Nature communications · 2024Article
- Targeting ROS production through inhibition of NADPH oxidases.Nature chemical biology · 2023Article
- 3D-Printable centrifugal devices for biomolecular solid state NMR rotors.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2023Article
- Structural conservation of HBV-like capsid proteins over hundreds of millions of years despite the shift from non-enveloped to enveloped life-style.Nature communications · 2023Article
- Molecular elucidation of drug-induced abnormal assemblies of the hepatitis B virus capsid protein by solid-state NMR.Nature communications · 2023Article
- Epitope Mapping and Binding Assessment by Solid-State NMR Provide a Way for the Development of Biologics under the Quality by Design Paradigm.Journal of the American Chemical Society · 2022Article
- Review
- Nucleic acid-protein interfaces studied by MAS solid-state NMR spectroscopy.Journal of structural biology: X · 2022Article
- Virus Structures and Dynamics by Magic-Angle Spinning NMR.Annual review of virology · 2021Review
- Spectroscopic glimpses of the transition state of ATP hydrolysis trapped in a bacterial DnaB helicase.Nature communications · 2021Article
- Solid-State NMR Studies of the Succinate-Acetate Permease from Citrobacter Koseri in Liposomes and Native Nanodiscs.Life (Basel, Switzerland) · 2021Article
- Evaluation of the Higher Order Structure of Biotherapeutics Embedded in Hydrogels for Bioprinting and Drug Release.Analytical chemistry · 2021Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Today, the sedimentation of proteins into a magic-angle spinning (MAS) rotor gives access to fast and reliable sample preparation for solid-state Nuclear Magnetic Resonance (NMR), and this has allowed for the investigation of a variety of non-crystalline protein samples. High protein concentrations on the order of 400 mg/mL can be achieved, meaning that around 50-60% of the NMR rotor content is protein; the rest is a buffer solution, which includes counter ions to compensate for the charge of the protein. We have demonstrated herein the long-term stability of four sedimented proteins and complexes thereof with nucleotides, comprising a bacterial DnaB helicase, an ABC transporter, an archaeal primase, and an RNA polymerase subunit. Solid-state NMR spectra recorded directly after sample filling and up to 5 years later indicated no spectral differences and no loss in signal intensity, allowing us to conclude that protein sediments in the rotor can be stable over many years. We have illustrated, using an example of an ABC transporter, that not only the structure is maintained, but that the protein is still functional after long-term storage in the sedimented state.
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