ArticleJournal of the American Chemical Society2013
Reduced native state stability in crowded cellular environment due to protein-protein interactions.
Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers, 1 of them a synthesis that pooled it.
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Who cites it
62 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Insight of the cytotoxicity of the aggregates of peptides or aberrant proteins: a meta-analysis.PloS one · 2014Pooled it
- PEG-mCherry interactions beyond classical macromolecular crowding.Protein science : a publication of the Protein Society · 2025Article
- BEMM-GEN: A Toolkit for Generating a Biomolecular Environment-Mimicking Model for Molecular Dynamics Simulation.Journal of chemical information and modeling · 2024Article
- Ribosome Tunnel Environment Drives the Formation of α-Helix during Cotranslational Folding.Journal of chemical information and modeling · 2024Article
- Computational Approaches to Predict Protein-Protein Interactions in Crowded Cellular Environments.Chemical reviews · 2024Review
- Article
- Glycosylation and Crowded Membrane Effects on Influenza Neuraminidase Stability and Dynamics.The journal of physical chemistry letters · 2023Article
- Molecular Basis for Actin Polymerization Kinetics Modulated by Solution Crowding.Biomolecules · 2023Article
- Varying molecular interactions explain aspects of crowder-dependent enzyme function of a viral protease.PLoS computational biology · 2023Article
- Activation of L-lactate oxidase by the formation of enzyme assemblies through liquid-liquid phase separation.Scientific reports · 2023Article
- Water Stress-Driven Changes in Bacterial Cell Surface Properties.Applied and environmental microbiology · 2022Article
- Modified Protein-Water Interactions in CHARMM36m for Thermodynamics and Kinetics of Proteins in Dilute and Crowded Solutions.Molecules (Basel, Switzerland) · 2022Article
- Evaluation of weak interactions of proteins and organic cations with DNA duplex structures.Biophysical journal · 2022Article
- Crowding-induced protein destabilization in the absence of soft attractions.Biophysical journal · 2022Article
- Protein assembly and crowding simulations.Current opinion in structural biology · 2022Review
- Computational Models for the Study of Protein Aggregation.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Crowding affects structural dynamics and contributes to membrane association of the NS3/4A complex.Biophysical journal · 2021Article
- Reduced efficacy of a Src kinase inhibitor in crowded protein solution.Nature communications · 2021Article
- Stability enhancement in a mAb and Fab coformulation.Scientific reports · 2020Article
- 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
2 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The effect of cellular crowding environments on protein structure and stability is a key issue in molecular and cellular biology. The classical view of crowding emphasizes the volume exclusion effect that generally favors compact, native states. Here, results from molecular dynamics simulations and NMR experiments show that protein crowders may destabilize native states via protein-protein interactions. In the model system considered here, mixtures of villin head piece and protein G at high concentrations, villin structures become increasingly destabilized upon increasing crowder concentrations. The denatured states observed in the simulation involve partial unfolding as well as more subtle conformational shifts. The unfolded states remain overall compact and only partially overlap with unfolded ensembles at high temperature and in the presence of urea. NMR measurements on the same systems confirm structural changes upon crowding based on changes of chemical shifts relative to dilute conditions. An analysis of protein-protein interactions and energetic aspects suggests the importance of enthalpic and solvation contributions to the crowding free energies that challenge an entropic-centered view of crowding effects.
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