ArticleACS omega2018
Mixed Macromolecular Crowding: A Protein and Solvent Perspective.
Article in ACS omega, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 59 citations in OpenAlex.
- Crowder-specific modulation of hepatitis C virus NS3/4A protease activity and local structural dynamics.Protein science : a publication of the Protein Society · 2026Article
- Covalent Network Formation Rate Controls Depletion-Induced Supramolecular Assembly in Hybrid Double Network Hydrogels.Angewandte Chemie (International ed. in English) · 2026Article
- Mimetics of in-cell and subcellular crowding and solvation for protein folding.Biochemical Society transactions · 2026Review
- Protein oxidation in crowded environments.The Biochemical journal · 2026Review
- Hydrodynamic Size Modulation of Exopolysaccharides fromJournal of microbiology and biotechnology · 2025Article
- A Computational Perspective to Intermolecular Interactions and the Role of the Solvent on Regulating Protein Properties.Chemical reviews · 2025Review
- Underestimated role of macromolecular crowding in bioengineeredMaterials today. Bio · 2025Article
- What determines sub-diffusive behavior in crowded protein solutions?Biophysical journal · 2024Article
- MeCP2-induced heterochromatin organization is driven by oligomerization-based liquid-liquid phase separation and restricted by DNA methylation.Nucleus (Austin, Tex.) · 2022Article
- Measuring Structural Changes in CytochromePolymers · 2022Article
- Electromechanical Photophysics of GFP Packed Inside Viral Protein Cages Probed by Force-Fluorescence Hybrid Single-Molecule Microscopy.Small (Weinheim an der Bergstrasse, Germany) · 2022Article
- Atomistic Simulation of Lysozyme in Solutions Crowded by Tetraethylene Glycol: Force Field Dependence.Molecules (Basel, Switzerland) · 2022Article
- Size-Dependent Interplay of Volume Exclusion Versus Soft Interactions: CytochromeFrontiers in molecular biosciences · 2022Article
- Transactivation domain of Adenovirus Early Region 1A (E1A): Investigating folding dynamics and aggregation.Current research in structural biology · 2022Article
- Article
- Capsicumicine, a New Bioinspired Peptide from Red Peppers Prevents Staphylococcal BiofilmMicrobiology spectrum · 2021Article
- Probing interactions of therapeutic antibodies with serum via second virial coefficient measurements.Biophysical journal · 2021Article
- Macromolecular crowding effects on the kinetics of opposing reactions catalyzed by alcohol dehydrogenase.Biochemistry and biophysics reports · 2021Article
- Structural Refolding and Thermal Stability of Myoglobin in the Presence of Mixture of Crowders: Importance of Various Interactions for Protein Stabilization in Crowded Conditions.Molecules (Basel, Switzerland) · 2021Article
- Effect of Different Crowding Agents on the Architectural Properties of the Bacterial Nucleoid-Associated Protein HU.International journal of molecular sciences · 2020Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the living cell, biomolecules perform their respective functions in the presence of not only one type of macromolecules but rather in the presence of various macromolecules with different shapes and sizes. In this study, we have investigated the effects of five single macromolecular crowding agents, Dextran 6, Dextran 40, Dextran 70, Ficoll 70, and PEG 8000 and their binary mixtures on the modulation in the domain separation of human serum albumin using a Förster resonance energy transfer-based approach and the translational mobility of a small fluorescent probe fluorescein isothiocyanate (FITC) using fluorescence correlation spectroscopy (FCS). Our observations suggest that mixed crowding induces greater cooperativity in the domain movement as compared to the components of the mixtures. Thermodynamic analyses of the same provide evidence of crossovers from enthalpy-based interactions to effects dominated by hard-sphere potential. When compared with those obtained for individual crowders, both domain movements and FITC diffusion studies show significant deviations from ideality, with an ideal solution being considered to be that arising from the sum of the contributions of those obtained in the presence of individual crowding agents. Considering the fact that domain movements are local (on the order of a few angstroms) in nature while translational movements span much larger lengthscales, our results imply that the observed deviation from simple additivity exists at several possible levels or lengthscales in such mixtures. Moreover, the nature and the type of deviation not only depend on the identities of the components of the crowder mixtures but are also influenced by the particular face of the serum protein (either the domain I-II or the domain II-III face) that the crowders interact with, thus providing further insights into the possible existence of microheterogeneities in such solutions.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.