ArticleProtein science : a publication of the Protein Society2008
The effects of macromolecular crowding on the mechanical stability of protein molecules.
Article in Protein science : a publication of the Protein Society, 2008. 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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Who cites it
27 citing papers in PubMed.
- Anthraquinones Inhibit Insulin Amyloidosis in Crowded Environments.Molecules (Basel, Switzerland) · 2026Article
- Structure and Dynamics of dsDNA in Cell-like Environments.Entropy (Basel, Switzerland) · 2022Review
- Electromechanical Photophysics of GFP Packed Inside Viral Protein Cages Probed by Force-Fluorescence Hybrid Single-Molecule Microscopy.Small (Weinheim an der Bergstrasse, Germany) · 2022Article
- Gap Junction-Mediated Delivery of Polymeric Macromolecules.ACS biomaterials science & engineering · 2022Article
- TAR RNA Mediated Folding of a Single-Arginine-Mutant HIV-1 Tat Protein within HeLa Cells Experiencing Intracellular Crowding.International journal of molecular sciences · 2021Article
- Protein nanomechanics in biological context.Biophysical reviews · 2021Review
- Interactions Under Crowding Milieu: Chemical-Induced Denaturation of Myoglobin is Determined by the Extent of Heme Dissociation on Interaction with Crowders.Biomolecules · 2020Article
- Carbohydrate-Based Macromolecular Crowding-Induced Stabilization of Proteins: Towards Understanding the Significance of the Size of the Crowder.Biomolecules · 2019Article
- Protein folding, binding, and droplet formation in cell-like conditions.Current opinion in structural biology · 2017Review
- Structure and Conformational Properties of d-Glucose/d-Galactose-Binding Protein in Crowded Milieu.Molecules (Basel, Switzerland) · 2017Article
- What macromolecular crowding can do to a protein.International journal of molecular sciences · 2014Review
- Computational modeling of the interplay between cadherin-mediated cell adhesion and Wnt signaling pathway.PloS one · 2014Article
- Article
- Force-induced unzipping transitions in an athermal crowded environment.The journal of physical chemistry. B · 2013Article
- Simulation and Modeling of Crowding Effects on the Thermodynamic and Kinetic Properties of Proteins with Atomic Details.Biophysical reviews · 2013Article
- Probing osmolyte participation in the unfolding transition state of a protein.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Power-law dependence of the melting temperature of ubiquitin on the volume fraction of macromolecular crowders.The Journal of chemical physics · 2011Article
- Macromolecular crowding remodels the energy landscape of a protein by favoring a more compact unfolded state.Journal of the American Chemical Society · 2010Article
- Correction of the viscous drag induced errors in macromolecular manipulation experiments using atomic force microscope.The Review of scientific instruments · 2010Article
- Rate theories for biologists.Quarterly reviews of biophysics · 2010Review
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Authors and funding
7 authors.
Funding
Abstract
Macromolecular crowding, a common phenomenon in the cellular environments, can significantly affect the thermodynamic and kinetic properties of proteins. A single-molecule method based on atomic force microscopy (AFM) was used to investigate the effects of macromolecular crowding on the forces required to unfold individual protein molecules. It was found that the mechanical stability of ubiquitin molecules was enhanced by macromolecular crowding from added dextran molecules. The average unfolding force increased from 210 pN in the absence of dextran to 234 pN in the presence of 300 g/L dextran at a pulling speed of 0.25 microm/sec. A theoretical model, accounting for the effects of macromolecular crowding on the native and transition states of the protein molecule by applying the scaled-particle theory, was used to quantitatively explain the crowding-induced increase in the unfolding force. The experimental results and interpretation presented could have wide implications for the many proteins that experience mechanical stresses and perform mechanical functions in the crowded environment of the cell.
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