ArticleScientific reports2016
Improved in-cell structure determination of proteins at near-physiological concentration.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 51 citations in OpenAlex.
- NMR Spectroscopy: Molecular Insights into Cell Wall Collapse and Oxidative Stress ofACS omega · 2026Article
- Side-chain-selective deuterium labeling by a simple bio-expression method enhances resolution and simplifies spectra inJournal of biomolecular NMR · 2025Article
- A temperature-driven DNA discrimination strategy to distinguish E. coli DNA and phage 5hmC-modified DNA.Nucleic acids research · 2025Article
- Identifying the minimal sets of distance restraints for FRET-assisted protein structural modeling.Protein science : a publication of the Protein Society · 2024Article
- Identifying the minimal sets of distance restraints for FRET-assisted protein structural modeling.ArXiv · 2024Article
- Progress, Challenges and Opportunities of NMR and XL-MS for Cellular Structural Biology.JACS Au · 2024Review
- Multi-Dimensional Structure and Dynamics Landscape of Proteins in Mammalian Cells Revealed by In-Cell NMR.Angewandte Chemie (International ed. in English) · 2023Article
- Protein structure determination in human cells by in-cell NMR and a reporter system to optimize protein delivery or transexpression.Communications biology · 2022Article
- The transient expression of recombinant proteins in plant cell packs facilitates stable isotope labelling for NMR spectroscopy.Plant biotechnology journal · 2022Article
- Visualizing Proteins in Mammalian Cells byAngewandte Chemie (International ed. in English) · 2022Article
- Radio Signals from Live Cells: The Coming of Age of In-Cell Solution NMR.Chemical reviews · 2022Review
- Spotlight on the Ballet of Proteins: The Structural Dynamic Properties of Proteins Illuminated by Solution NMR.International journal of molecular sciences · 2020Review
- Observation of nucleic acids inside living human cells by in-cell NMR spectroscopy.Biophysics and physicobiology · 2020Article
- Emerging solution NMR methods to illuminate the structural and dynamic properties of proteins.Current opinion in structural biology · 2019Review
- Smad7 Binds Differently to Individual and Tandem WW3 and WW4 Domains of WWP2 Ubiquitin Ligase Isoforms.International journal of molecular sciences · 2019Article
- Protein Structure Determination in Living Cells.International journal of molecular sciences · 2019Review
- Interaction proteomics by using in-cell NMR spectroscopy.Journal of proteomics · 2019Review
- Improved sensitivity and resolution of in-cell NMR spectra.Methods in enzymology · 2019Article
- Protein Tertiary Structure by Crosslinking/Mass Spectrometry.Trends in biochemical sciences · 2018Review
- NMR of Macromolecular Assemblies and Machines at 1 GHz and Beyond: New Transformative Opportunities for Molecular Structural Biology.Methods in molecular biology (Clifton, N.J.) · 2018Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Investigating three-dimensional (3D) structures of proteins in living cells by in-cell nuclear magnetic resonance (NMR) spectroscopy opens an avenue towards understanding the structural basis of their functions and physical properties under physiological conditions inside cells. In-cell NMR provides data at atomic resolution non-invasively, and has been used to detect protein-protein interactions, thermodynamics of protein stability, the behavior of intrinsically disordered proteins, etc. in cells. However, so far only a single de novo 3D protein structure could be determined based on data derived only from in-cell NMR. Here we introduce methods that enable in-cell NMR protein structure determination for a larger number of proteins at concentrations that approach physiological ones. The new methods comprise (1) advances in the processing of non-uniformly sampled NMR data, which reduces the measurement time for the intrinsically short-lived in-cell NMR samples, (2) automatic chemical shift assignment for obtaining an optimal resonance assignment, and (3) structure refinement with Bayesian inference, which makes it possible to calculate accurate 3D protein structures from sparse data sets of conformational restraints. As an example application we determined the structure of the B1 domain of protein G at about 250 μM concentration in living E. coli cells.
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