ArticleJournal of molecular biology2008
Molecular crowding inhibits intramolecular breathing motions in proteins.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 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
50 citing papers in PubMed.
- Simulating Crowding In Vitro: Not an Elusive Goal Any Longer.Sub-cellular biochemistry · 2025Review
- Study of novel androgen receptor V770 variant in androgen insensitivity syndrome patients reveals the transitional state of the androgen receptor ligand binding domain homodimer.Protein science : a publication of the Protein Society · 2023Article
- Strategies for the Production of Molecular Animations.Frontiers in bioinformatics · 2022Review
- Hantaviruses use the endogenous host factor P58IPK to combat the PKR antiviral response.PLoS pathogens · 2021Article
- Ultrafast coherent motion and helix rearrangement of homodimeric hemoglobin visualized with femtosecond X-ray solution scattering.Nature communications · 2021Article
- A small sustained increase in NOD1 abundance promotes ligand-independent inflammatory and oncogene transcriptional responses.Science signaling · 2020Article
- Machine learning deciphers structural features of RNA duplexes measured with solution X-ray scattering.IUCrJ · 2020Article
- Global and local envelope protein dynamics of hepatitis C virus determine broad antibody sensitivity.Science advances · 2020Article
- Phosphoinositides regulate force-independent interactions between talin, vinculin, and actin.eLife · 2020Article
- Gelatin and Starch: What Better Stabilizes the Enzyme Activity?Doklady biological sciences : proceedings of the Academy of Sciences of the USSR, Biological sciences sections · 2020Article
- Salt Dependence of A-Form RNA Duplexes: Structures and Implications.The journal of physical chemistry. B · 2019Article
- Hypervariable region 1 and N-linked glycans of hepatitis C regulate virion neutralization by modulating envelope conformations.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Review
- Post-translational Protein Acetylation: An Elegant Mechanism for Bacteria to Dynamically Regulate Metabolic Functions.Frontiers in microbiology · 2019Review
- Predicting X-ray solution scattering from flexible macromolecules.Protein science : a publication of the Protein Society · 2018Article
- Crowding in Cellular Environments at an Atomistic Level from Computer Simulations.The journal of physical chemistry. B · 2017Article
- Weak protein-protein interactions in live cells are quantified by cell-volume modulation.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Modulation of hemoglobin dynamics by an allosteric effector.Protein science : a publication of the Protein Society · 2017Article
- Sulfmyoglobin Conformational Change: A Role in the Decrease of Oxy-Myoglobin Functionality.Biochemistry and biophysics reports · 2016Article
- Modulation of HIV protease flexibility by the T80N mutation.Proteins · 2015Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
In aqueous solution some proteins undergo large-scale movements of secondary structures, subunits or domains, referred to as protein "breathing", that define a native-state ensemble of structures. These fluctuations are sensitive to the nature and concentration of solutes and other proteins and are thereby expected to be different in the crowded interior of a cell than in dilute solution. Here we use a combination of wide angle X-ray scattering (WAXS) and computational modeling to derive a quantitative measure of the spatial scale of conformational fluctuations in a protein solution. Concentration-dependent changes in the observed scattering intensities are consistent with a model of structural fluctuations in which secondary structures undergo rigid-body motions relative to one another. This motion increases with decreasing protein concentration or increasing temperature. Analysis of a set of five structurally and functionally diverse proteins reveals a diversity of kinetic behaviors. Proteins with multiple disulfide bonds exhibit little or no increase in breathing in dilute solutions. The spatial extent of structural fluctuations appears highly dependent on both protein structure and concentration and is universally suppressed at very high protein concentrations.
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Registered trials
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