ArticleThe Journal of chemical physics2011
Power-law dependence of the melting temperature of ubiquitin on the volume fraction of macromolecular crowders.
Article in The Journal of chemical physics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Quantification of excluded volume effects on the folding landscape of Pseudomonas aeruginosa apoazurin in vitro.Biophysical journal · 2013Article
- Reaching new levels of realism in modeling biological macromolecules in cellular environments.Journal of molecular graphics & modelling · 2013Review
- Article
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2 authors.
Funding
Abstract
The dependence of the melting temperature increase (ΔT(m)) of the protein ubiquitin on the volume fraction (ϕ) of several commonly used macromolecular crowding agents (dextran 6, 40, and 70 and ficoll 70) was quantitatively examined and compared to a recently developed theoretical crowding model, i.e., ΔT(m) ∼ (R(g)∕R(c))(α)φ(α∕3). We found that in the current case this model correctly predicts the power-law dependence of ΔT(m) on φ but significantly overestimates the role of the size (i.e., R(c)) of the crowding agent. In addition, we found that for ubiquitin the exponent α is in the range of 4.1-6.5, suggesting that the relation of α=3∕(3ν-1) is a better choice for estimating α based on the Flory coefficient (ν) of the polypeptide chain. Taken together these findings highlight the importance of improving our knowledge and theoretical treatment of the microcompartmentalization of the commonly used model crowding agents.
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