ArticleThe European physical journal. E, Soft matter2010
Molecular dynamics simulations of cytochrome c unfolding in AOT reverse micelles: The first steps.
Article in The European physical journal. E, Soft matter, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 38 citations in OpenAlex.
- The Size of AOT Reverse Micelles.The journal of physical chemistry. B · 2016Article
- Two-dimensional heterospectral correlation analysis of the redox-induced conformational transition in cytochrome c using surface-enhanced Raman and infrared absorption spectroscopies on a two-layer gold surface.The journal of physical chemistry. B · 2013Article
- Low-temperature molecular dynamics simulations of horse heart cytochrome c and comparison with inelastic neutron scattering data.European biophysics journal : EBJ · 2013Article
- Simulations of the confinement of ubiquitin in self-assembled reverse micelles.The Journal of chemical physics · 2011Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
This paper explores the reduced form of horse cytochrome c confined in reverse micelles (RM) of sodium bis-(2-ethylhexyl) sulfosuccinate (AOT) in isooctane by molecular dynamics simulation. RMs of two sizes were constructed at a water content of W (o) = [ H₂O ]/[AOT] = 5.5 and 9.1. Our results show that the protein secondary structure and the heme conformation both depend on micellar hydration. At low hydration, the protein structure and the heme moiety remain stable, whereas at high water content the protein becomes unstable and starts to unfold. At W (o) = 9.1 , according to the X-ray structure, conformational changes are mainly localized on protein loops and around the heme moiety, where we observe a partial opening of the heme crevice. These findings suggest that within our time window (10ns), the structural changes observed at the heme level are the first steps of the protein denaturation process, previously described experimentally in micellar solutions. In addition, a specific binding of AOT molecules to a few lysine residues of the protein was found only in the small-sized RM.
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