ArticlePloS one2013
Denatured state structural property determines protein stabilization by macromolecular crowding: a thermodynamic and structural approach.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 59 citations in OpenAlex.
- A new fibrillization mechanism of β-lactoglobulin in glycine solutions.International journal of biological macromolecules · 2022Article
- Crowding-induced protein destabilization in the absence of soft attractions.Biophysical journal · 2022Article
- Quantification of Entropic Excluded Volume Effects Driving Crowding-Induced Collapse and Folding of a Disordered Protein.The journal of physical chemistry letters · 2022Article
- Structural basis of peroxidase catalytic cycle of human Prdx6.Scientific reports · 2020Article
- Effects of Ethylene Glycol on the Structure and Stability of Myoglobin Using Spectroscopic, Interaction, andACS omega · 2020Article
- Interactions Under Crowding Milieu: Chemical-Induced Denaturation of Myoglobin is Determined by the Extent of Heme Dissociation on Interaction with Crowders.Biomolecules · 2020Article
- Measuring the effects of macromolecular crowding on antibody function with biolayer interferometry.mAbs · 2019Article
- Carbohydrate-Based Macromolecular Crowding-Induced Stabilization of Proteins: Towards Understanding the Significance of the Size of the Crowder.Biomolecules · 2019Article
- An optimized strategy to measure protein stability highlights differences between cold and hot unfolded states.Nature communications · 2017Article
- Protein Composition Determines the Effect of Crowding on the Properties of Disordered Proteins.Biophysical journal · 2016Article
- The Differential Response of Proteins to Macromolecular Crowding.PLoS computational biology · 2016Article
- Calcineurin in a Crowded World.Biochemistry · 2016Article
- Article
- An overview of technologies for immobilization of enzymes and surface analysis techniques for immobilized enzymes.Biotechnology, biotechnological equipment · 2015Article
- What macromolecular crowding can do to a protein.International journal of molecular sciences · 2014Review
- Macromolecular crowding induces holo α-lactalbumin aggregation by converting to its apo form.PloS one · 2014Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Understanding of protein structure and stability gained to date has been acquired through investigations made under dilute conditions where total macromolecular concentration never surpasses 10 g l(-1). However, biological macromolecules are known to evolve and function under crowded intracellular environments that comprises of proteins, nucleic acids, ribosomes and carbohydrates etc. Crowded environment is known to result in altered biological properties including thermodynamic, structural and functional aspect of macromolecules as compared to the macromolecules present in our commonly used experimental dilute buffers (for example, Tris HCl or phosphate buffer). In this study, we have investigated the thermodynamic and structural consequences of synthetic crowding agent (Ficoll 70) on three different proteins (Ribonuclease-A, lysozyme and holo α-lactalbumin) at different pH values. We report here that the effect of crowding is protein dependent in terms of protein thermal stability and structure. We also observed that the structural characteristics of the denatured state determines if crowding will have an effect or not on the protein stability.
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