ArticleJournal of molecular modeling2018
Exploring the differences and similarities between urea and thermally driven denaturation of bovine serum albumin: intermolecular forces and solvation preferences.
Article in Journal of molecular modeling, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 36 citations in OpenAlex.
- Comparative unfolding of the Trp-cage miniprotein in anionic and cationic surfactants.PloS one · 2026Article
- Novel computational and drug design strategies for inhibition of human papillomavirus-associated cervical cancer and DNA polymerase theta receptor by Apigenin derivatives.Scientific reports · 2023Article
- Changing mechanical properties of photopolymerized, dityrosine-crosslinked protein-based hydrogels.Frontiers in bioengineering and biotechnology · 2022Article
- In Silico Characterization of the Binding Modes of Surfactants with Bovine Serum Albumin.Scientific reports · 2019Article
- Prediction of membrane separation efficiency for hydrophobic and hydrophilic proteins : A coarse-grained Brownian dynamics simulation study.Journal of molecular modeling · 2019Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The interactions of bovine serum albumin (BSA) with urea/water were investigated by computer simulation. It was revealed that the BSA-hydrophobic residues in urea solutions favored contact with urea more than with water. Energy decomposition analysis showed that van der Waals energy was the dominant driving force behind urea affinity for hydrophobic residues, whereas coulombic attraction was largely responsible for water affinity for these residues. Meanwhile, urea-BSA hydrogen bond energies were found to be weaker than water-BSA hydrogen bond energies. The greater strength of water-BSA hydrogen bonds than urea-BSA hydrogen bonds, and the opposing preferential interaction between the BSA and urea suggest that disruption of hydrophobic interaction predominates urea-protein denaturation. In pure water, hydrophobic residues showed aggregation tendencies at 323 K, suggesting an increase in hydrophobicity, while at 353 K the residues were partly denatured due to loss of hydrogen bonds; thus, disruption of hydrophobic interactions appeared to contribute less to thermal denaturation.
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Registered trials
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