ArticleBiophysical journal1997
19F NMR measurements of the rotational mobility of proteins in vivo.
Article in Biophysical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
27 citing papers in PubMed, 95 citations in OpenAlex.
- Enzyme stabilisation due to incorporation of a fluorinated non-natural amino acid at the protein surface.Scientific reports · 2024Article
- Direct Observation of Membrane-Associated H-Ras in the Native Cellular Environment by In-CellJACS Au · 2023Article
- Resolving molecular diffusion and aggregation of antibody proteins with megahertz X-ray free-electron laser pulses.Nature communications · 2022Article
- Radio Signals from Live Cells: The Coming of Age of In-Cell Solution NMR.Chemical reviews · 2022Review
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- Ribosome-Amplified Metabolism, RAMBO, Measured by NMR Spectroscopy.Biochemistry · 2021Article
- In-cell Solid-State NMR Studies of Antimicrobial Peptides.Frontiers in medical technology · 2020Review
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- In-Cell NMR Spectroscopy of Intrinsically Disordered Proteins.Proteomics · 2019Review
- Improved sensitivity and resolution of in-cell NMR spectra.Methods in enzymology · 2019Article
- Slow-Down in Diffusion in Crowded Protein Solutions Correlates with Transient Cluster Formation.The journal of physical chemistry. B · 2017Article
- Hallmarks of Reversible Separation of Living, Unperturbed Cell Membranes into Two Liquid Phases.Biophysical journal · 2017Article
- Evaluating electronic structure methods for accurate calculation ofJournal of computational chemistry · 2017Article
- A cell is more than the sum of its (dilute) parts: A brief history of quinary structure.Protein science : a publication of the Protein Society · 2017Review
- Disordered Protein Diffusion under Crowded Conditions.The journal of physical chemistry letters · 2012Article
- Water-exclusion and liquid-structure forces in implicit solvation.The journal of physical chemistry. B · 2011Article
- Site-specific ¹⁹F NMR chemical shift and side chain relaxation analysis of a membrane protein labeled with an unnatural amino acid.Protein science : a publication of the Protein Society · 2011Article
- NMR protein structure determination in living E. coli cells using nonlinear sampling.Nature protocols · 2010Article
- Protein folding stability and dynamics imaged in a living cell.Nature methods · 2010Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Three glycolytic enzymes, hexokinase, phosphoglycerate kinase, and pyruvate kinase, were fluorine labeled in the yeast Saccharomyces cerevisiae by biosynthetic incorporation of 5-fluorotryptophan. 19F NMR longitudinal relaxation time measurements on the labeled enzymes were used to assess their rotational mobility in the intact cell. Comparison with the results obtained from relaxation time measurements of the purified enzymes in vitro and from theoretical calculations showed that two of the labeled enzymes, phosphoglycerate kinase and hexokinase, were tumbling in a cytoplasm that had a viscosity approximately twice that of water. There were no detectable signals from pyruvate kinase in vivo, although it could be detected in diluted cell extracts, indicating that there was some degree of motional restriction of the enzyme in the intact cell.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.