ArticleNature2009
Protein structure determination in living cells by in-cell NMR spectroscopy.
Article in Nature, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 143 papers.
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Who cites it
143 citing papers in PubMed.
- High-resolution NMR spectroscopy of proteins in intact mitochondria.Nature chemical biology · 2026Article
- In-cell NMR spectroscopy: advancements, applications, challenges, and future directions in structural biology.Magma (New York, N.Y.) · 2026Review
- In vitro, cellular and in vivo studies of amyloid oligomers structure and toxicity: Challenges and advances.Protein science : a publication of the Protein Society · 2026Review
- Limited proteolysis-coupled mass spectrometry captures proteome-wide protein structural alterations and biomolecular condensation in living cells.Molecular systems biology · 2026Article
- Live Metabolomics with NMR.Analytical chemistry · 2026Review
- Computational and Experimental Approaches and Applications of Biological NMR.Advances in experimental medicine and biology · 2026Review
- A Controlled System for Parahydrogen Hyperpolarization Experiments.Molecules (Basel, Switzerland) · 2025Article
- Multiscale theoretical study of infrared spectroscopy for the thermal denaturation process of aprotinin.Journal of molecular modeling · 2025Article
- Periplasmic protein quality control at atomic level in live cells.Nature communications · 2025Article
- Multistate Structure Determination and Dynamics Analysis Reveals a Unique Ubiquitin-Recognition Mechanism in Ubiquitin C-terminal Hydrolase.Journal of the American Chemical Society · 2025Article
- Target Engagement Assays in Early Drug Discovery.Journal of medicinal chemistry · 2025Review
- An approach to characterize mechanisms of action of anti-amyloidogenic compounds in vitro and in situ.NPJ Parkinson's disease · 2025Article
- Stability of the polarization agent AsymPolPOK in intact and lysed mammalian cells.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2025Article
- Identifying the minimal sets of distance restraints for FRET-assisted protein structural modeling.Protein science : a publication of the Protein Society · 2024Article
- From molecular descriptions to cellular functions of intrinsically disordered protein regions.Biophysics reviews · 2024Review
- An Efficient and Stable Polarizing Agent for In-Cell Magic-Angle Spinning Dynamic Nuclear Polarization NMR Spectroscopy.The journal of physical chemistry letters · 2024Article
- Stability of the polarization agent AsymPolPOK in intact and lysed mammalian cells.bioRxiv : the preprint server for biology · 2024Article
- Using in vivo intact structure for system-wide quantitative analysis of changes in proteins.Nature communications · 2024Article
- Identifying the minimal sets of distance restraints for FRET-assisted protein structural modeling.ArXiv · 2024Article
- DNP-assisted solid-state NMR enables detection of proteins at nanomolar concentrations in fully protonated cellular milieu.Journal of biomolecular NMR · 2024Article
83 more citing papers are in PubMed but not listed here.
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Authors and funding
14 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Investigating proteins 'at work' in a living environment at atomic resolution is a major goal of molecular biology, which has not been achieved even though methods for the three-dimensional (3D) structure determination of purified proteins in single crystals or in solution are widely used. Recent developments in NMR hardware and methodology have enabled the measurement of high-resolution heteronuclear multi-dimensional NMR spectra of macromolecules in living cells (in-cell NMR). Various intracellular events such as conformational changes, dynamics and binding events have been investigated by this method. However, the low sensitivity and the short lifetime of the samples have so far prevented the acquisition of sufficient structural information to determine protein structures by in-cell NMR. Here we show the first, to our knowledge, 3D protein structure calculated exclusively on the basis of information obtained in living cells. The structure of the putative heavy-metal binding protein TTHA1718 from Thermus thermophilus HB8 overexpressed in Escherichia coli cells was solved by in-cell NMR. Rapid measurement of the 3D NMR spectra by nonlinear sampling of the indirectly acquired dimensions was used to overcome problems caused by the instability and low sensitivity of living E. coli samples. Almost all of the expected backbone NMR resonances and most of the side-chain NMR resonances were observed and assigned, enabling high quality (0.96 ångström backbone root mean squared deviation) structures to be calculated that are very similar to the in vitro structure of TTHA1718 determined independently. The in-cell NMR approach can thus provide accurate high-resolution structures of proteins in living environments.
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