ArticlePloS one2014
Denatured mammalian protein mixtures exhibit unusually high solubility in nucleic acid-free pure water.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- In the Beginning: Let Hydration Be Coded in Proteins for Manifestation and Modulation by Salts and Adenosine Triphosphate.International journal of molecular sciences · 2024Review
- Hydrophobicity and molecular mass-based separation method for autoantibody discovery from mammalian total cellular proteins.Protein science : a publication of the Protein Society · 2023Article
- Adenosine triphosphate energy-independently controls protein homeostasis with unique structure and diverse mechanisms.Protein science : a publication of the Protein Society · 2021Review
- Nucleic acids in inclusion bodies obtained from E. coli cells expressing human interferon-gamma.Microbial cell factories · 2020Article
- Environment-transformable sequence-structure relationship: a general mechanism for proteotoxicity.Biophysical reviews · 2018Review
- Evaluation of irreversible protein thermal inactivation caused by breakage of disulphide bonds using methanethiosulphonate.Scientific reports · 2017Article
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Authors and funding
9 authors.
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Abstract
Preventing protein aggregation is a major goal of biotechnology. Since protein aggregates are mainly comprised of unfolded proteins, protecting against denaturation is likely to assist solubility in an aqueous medium. Contrary to this concept, we found denatured total cellular protein mixture from mammalian cell kept high solubility in pure water when the mixture was nucleic acids free. The lysates were prepared from total cellular protein pellet extracted by using guanidinium thiocyanate-phenol-chloroform mixture of TRIzol, denatured and reduced total protein mixtures remained soluble after extensive dialysis against pure water. The total cell protein lysates contained fully disordered proteins that readily formed large aggregates upon contact with nucleic acids or salts. These findings suggested that the highly flexible mixtures of disordered proteins, which have fully ionized side chains, are protected against aggregation. Interestingly, this unusual solubility is characteristic of protein mixtures from higher eukaryotes, whereas most prokaryotic protein mixtures were aggregated under identical conditions. This unusual solubility of unfolded protein mixtures could have implications for the study of intrinsically disordered proteins in a variety of cells.
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