ArticleBiochemistry2011
Exploring weak, transient protein--protein interactions in crowded in vivo environments by in-cell nuclear magnetic resonance spectroscopy.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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Who cites it
64 citing papers in PubMed, 160 citations in OpenAlex.
- Real-time NMR monitoring of HMF biotransformation by Ectopseudomonas oleovorans CECT 5344 R1D.Applied microbiology and biotechnology · 2026Article
- Quantifying Protein Homodimer Affinities and the Effect of Molecular Glues and Interface Residues Using Native Mass Spectrometry.Journal of the American Chemical Society · 2026Article
- Crowding-induced stabilization and destabilization in a single protein.Protein science : a publication of the Protein Society · 2025Article
- Ubiquitin's Conformational Heterogeneity as Discerned by Nuclear Magnetic Resonance Spectroscopy.Chembiochem : a European journal of chemical biology · 2024Review
- Probing Electrostatic and Hydrophobic Associative Interactions in Cells.The journal of physical chemistry. B · 2024Article
- Analysis of Fluorescent Proteins for Observing Single Gene Locus in a Live and FixedThe journal of physical chemistry. B · 2024Article
- Intracellular environment can change protein conformational dynamics in cells through weak interactions.Science advances · 2023Article
- Characterizing Transient Protein-Protein Interactions by Trp-Cys Quenching and Computer Simulations.The journal of physical chemistry letters · 2022Article
- NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins.Chemical reviews · 2022Review
- Radio Signals from Live Cells: The Coming of Age of In-Cell Solution NMR.Chemical reviews · 2022Review
- Physicochemical classification of organisms.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Atomistic Simulation of Lysozyme in Solutions Crowded by Tetraethylene Glycol: Force Field Dependence.Molecules (Basel, Switzerland) · 2022Article
- Preferential Interactions of a Crowder Protein with the Specific Binding Site of a Native Protein Complex.The journal of physical chemistry letters · 2022Article
- PCSK9 as a Target for Development of a New Generation of Hypolipidemic Drugs.Molecules (Basel, Switzerland) · 2022Review
- GalaxyHeteromer: protein heterodimer structure prediction by template-based and ab initio docking.Nucleic acids research · 2021Article
- Connecting Longitudinal and Transverse Relaxation Rates in Live-Cell NMR.The journal of physical chemistry. B · 2020Article
- All atom insights into the impact of crowded environments on protein stability by NMR spectroscopy.Nature communications · 2020Article
- Diffusive protein interactions in human versus bacterial cells.Current research in structural biology · 2020Article
- Article
- Clustering and dynamics of crowded proteins near membranes and their influence on membrane bending.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
4 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Biology relies on functional interplay of proteins in the crowded and heterogeneous environment inside cells, and functional protein interactions are often weak and transient. Thus, methods that preserve these interactions and provide information about them are needed. In-cell nuclear magnetic resonance (NMR) spectroscopy is an attractive method for studying a protein's behavior in cells because it may provide residue-level structural and dynamic information, yet several factors limit the feasibility of protein NMR spectroscopy in cells; among them, slow rotational diffusion has emerged as the most important. In this paper, we seek to elucidate the causes of the dramatically slow protein tumbling in cells and in so doing to gain insight into how the intracellular viscosity and weak, transient interactions modulate protein mobility. To address these questions, we characterized the rotational diffusion of three model globular proteins in Escherichia coli cells using two-dimensional heteronuclear NMR spectroscopy. These proteins have a similar molecular size and globular fold but very different surface properties, and indeed, they show very different rotational diffusion in the E. coli intracellular environment. Our data are consistent with an intracellular viscosity approximately 8 times that of water, too low to be a limiting factor for observation of small globular proteins by in-cell NMR spectroscopy. Thus, we conclude that transient interactions with cytoplasmic components significantly and differentially affect the mobility of proteins and therefore their NMR detectability. Moreover, we suggest that an intricate interplay of total protein charge and hydrophobic interactions plays a key role in regulating these weak intermolecular interactions in cells.
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Registered trials
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