ArticleBiophysical journal2008
Free energy of sickle hemoglobin polymerization: a scaled-particle treatment for use with dextran as a crowding agent.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- The Effect of Attractive Interactions and Macromolecular Crowding on Crystallins Association.PloS one · 2016Article
- Wanted: scalable tracers for diffusion measurements.The journal of physical chemistry. B · 2014Review
- An FFT-based method for modeling protein folding and binding under crowding: benchmarking on ellipsoidal and all-atom crowders.Journal of chemical theory and computation · 2013Article
- Contrasting factors on the kinetic path to protein complex formation diminish the effects of crowding agents.Biophysical journal · 2012Article
- The molecular refractive function of lens γ-Crystallins.Journal of molecular biology · 2011Article
- The role of macromolecular crowding in the evolution of lens crystallins with high molecular refractive index.Physical biology · 2011Article
- Power-law dependence of the melting temperature of ubiquitin on the volume fraction of macromolecular crowders.The Journal of chemical physics · 2011Article
- Nonadditive effects of mixed crowding on protein stability.Proteins · 2009Article
- Effect of macromolecular crowding on protein binding stability: modest stabilization and significant biological consequences.Biophysical journal · 2009Article
- Crowding effects of membrane proteins.The journal of physical chemistry. B · 2009Article
- The effects of macromolecular crowding on the mechanical stability of protein molecules.Protein science : a publication of the Protein Society · 2008Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fundamental to the analysis of protein polymerization is the free energy of association, typically determined from solubility. It has been previously shown that concentrated 70 kDa dextran lowers the solubility of sickle hemoglobin, due to molecular crowding, and provides a useful ranking tool for the effects of inhibitors and molecular modifications. Because hemoglobin occupies a substantial volume as well, crowding effects of both hemoglobin and dextran contribute to the nonideality of the solution. We show how scaled-particle theory can be used to account for both types of crowding, thus allowing the determination of solubility in the absence of dextran, given data measured in its presence. The approach adopted approximates dextran as a sphere with a volume that decreases as the concentration of dextran increases. We use an asymptotic relation to describe the volume, which decreases nearly linearly by a factor of two over the range studied, from 60 to 230 mg/ml. This compression is similar to previously observed compression of sephadex beads and ficoll solutions. In the limit of low hemoglobin concentrations, the theory reduces to the previously-used approach of Ogston. Our method therefore provides a means of measuring the free energy of association of molecules that occupy significant volume fractions, even when assisted by the crowding of dextran and we present a tabulation of all known free energies of polymerization of sickle hemoglobin measured in the presence of dextran.
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