ArticleBiomolecules2020
Interactions Under Crowding Milieu: Chemical-Induced Denaturation of Myoglobin is Determined by the Extent of Heme Dissociation on Interaction with Crowders.
Article in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 38 citations in OpenAlex.
- Preserving enzyme conformation and catalytic efficiency in crowded and active environments.Nanoscale advances · 2025Article
- Unveiling the Catalytic Roles ofMolecules (Basel, Switzerland) · 2024Article
- What determines sub-diffusive behavior in crowded protein solutions?Biophysical journal · 2024Article
- Time-Resolved X-ray Observation of Intracellular Crystallized Protein in Living Animal.International journal of molecular sciences · 2023Article
- Size-Dependent Interplay of Volume Exclusion Versus Soft Interactions: CytochromeFrontiers in molecular biosciences · 2022Article
- Protein folding mechanism revealed by single-molecule force spectroscopy experiments.Biophysics reports · 2021Article
- Macromolecular crowding modulates α-synuclein amyloid fiber growth.Biophysical journal · 2021Article
- Macromolecular crowding effects on the kinetics of opposing reactions catalyzed by alcohol dehydrogenase.Biochemistry and biophysics reports · 2021Article
- Quantitative evaluation of macromolecular crowding environment based on translational and rotational diffusion using polarization dependent fluorescence correlation spectroscopy.Scientific 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
- Interaction of polyethylene glycol with cytochrome c investigated via in vitro and in silico approaches.Scientific reports · 2021Article
- Response to crowded conditions reveals compact nucleus for amyloid formation of folded protein.QRB discovery · 2021Article
- Combined Effects of Confinement and Macromolecular Crowding on Protein Stability.International journal of molecular sciences · 2020Article
- Biophysical Elucidation of Fibrillation Inhibition by Sugar Osmolytes in α-Lactalbumin: Multispectroscopic and Molecular Docking Approaches.ACS omega · 2020Article
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
Generally, in vivo function and structural changes are studied by probing proteins in a dilute solution under in vitro conditions, which is believed to be mimicking proteins in intracellular milieu. Earlier, thermal-induced denaturation of myoglobin, in the milieu of crowder molecule showed destabilization of the metal protein. Destabilization of protein by thermal-induced denaturation involves a large extrapolation, so, the reliability is questionable. This led us to measure the effects of macromolecular crowding on its stability by chemical-induced denaturation of the protein using probes like circular dichroism and absorption spectroscopy in the presence of dextran 70 and ficoll 70 at various pHs (acidic: 6.0, almost neutral:7.0 and basic: 8.0). Observations showed that the degree of destabilization of myoglobin was greater due to ficoll 70 as compared to that of dextran 70 so it can be understood that the nature of the crowder or the shape of the crowder has an important role towards the stability of proteins. Additionally, the degree of destabilization was observed as pH dependent, however the pH dependence is different for different crowders. Furthermore, isothermal titration calorimetry and molecular docking studies confirmed that both the crowders (ficoll and dextran) bind to heme moiety of myoglobin and a single binding site was observed for each.
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