ArticleBiopolymers2015
Separating chemical and excluded volume interactions of polyethylene glycols with native proteins: Comparison with PEG effects on DNA helix formation.
Article in Biopolymers, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Differences and Similarities in Protein and Nucleic Acid Structures and Their Biological Interactions.Current issues in molecular biology · 2025Review
- Hidden water's influence on rhodopsin activation.Biophysical journal · 2024Review
- Elucidating the Role of Groove Hydration on Stability and Functions of Biased DNA Duplexes in Cell-Like Chemical Environments.Journal of the American Chemical Society · 2024Article
- Hydrodynamic and thermodynamic analysis of PEGylated human serum albumin.Biophysical journal · 2024Article
- The molecular basis for hydrodynamic properties of PEGylated human serum albumin.Biophysical journal · 2024Article
- Excluded Volume and Weak Interactions in Crowded Solutions Modulate Conformations and RNA Binding of an Intrinsically Disordered Tail.The journal of physical chemistry. B · 2023Article
- Crowded environments tune the fold-switching in metamorphic proteins.Communications chemistry · 2023Article
- Crowding-induced phase separation and gelling by co-condensation of PEG in NPM1-rRNA condensates.Biophysical journal · 2023Article
- Hydration-mediated G-protein-coupled receptor activation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- All atom insights into the impact of crowded environments on protein stability by NMR spectroscopy.Nature communications · 2020Article
- Crowder-Induced Conformational Ensemble Shift in Escherichia coli Prolyl-tRNA Synthetase.Biophysical journal · 2019Article
- Isotonic concentrations of excipients control the dimerization rate of a therapeutic immunoglobulin G1 antibody during refrigerated storage based on their rank order of native-state interaction.Protein science : a publication of the Protein Society · 2018Article
- Protein shape modulates crowding effects.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Towards developing principles of protein folding and dynamics in the cell.Physical biology · 2018Review
- Toward an understanding of biochemical equilibria within living cells.Biophysical reviews · 2018Review
- Large cosolutes, small cosolutes, and dihydrofolate reductase activity.Protein science : a publication of the Protein Society · 2017Article
- Observed crowding effects on Mycobacterium tuberculosis 2-trans-enoyl-ACP (CoA) reductase enzyme activity are not due to excluded volume only.Scientific reports · 2017Article
- Experimental Atom-by-Atom Dissection of Amide-Amide and Amide-Hydrocarbon Interactions in HJournal of the American Chemical Society · 2017Article
- Cosolutes, Crowding, and Protein Folding Kinetics.The journal of physical chemistry. B · 2017Article
- Cosolute and Crowding Effects on a Side-By-Side Protein Dimer.Biochemistry · 2017Article
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3 authors.
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Abstract
Small and large PEGs greatly increase chemical potentials of globular proteins (μ2), thereby favoring precipitation, crystallization, and protein-protein interactions that reduce water-accessible protein surface and/or protein-PEG excluded volume. To determine individual contributions of PEG-protein chemical and excluded volume interactions to μ2 as functions of PEG molality m3 , we analyze published chemical potential increments μ23 = dμ2/dm3 quantifying unfavorable interactions of PEG (PEG200-PEG6000) with BSA and lysozyme. For both proteins, μ23 increases approximately linearly with the number of PEG residues (N3). A 1 molal increase in concentration of PEG -CH2 OCH2 - groups, for any chain-length PEG, increases μBSA by ∼2.7 kcal/mol and μlysozyme by ∼1.0 kcal/mol. These values are similar to predicted chemical interactions of PEG -CH2 OCH2 - groups with these protein components (BSA ∼3.3 kcal/mol, lysozyme ∼0.7 kcal/mol), dominated by unfavorable interactions with amide and carboxylate oxygens and counterions. While these chemical effects should be dominant for small PEGs, larger PEGS are expected to exhibit unfavorable excluded volume interactions and reduced chemical interactions because of shielding of PEG residues in PEG flexible coils. We deduce that these excluded volume and chemical shielding contributions largely compensate, explaining why the dependence of μ23 on N3 is similar for both small and large PEGs.
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