Cytochrome-c in reverse micelles: Small angle x-ray scattering measurements, percolation process, and critical behavior: An interpretation with an association model

Cassin, G.; Duda, Yurko; Holovko, M.; Badiali, J.P.; Piléni, M. P.

doi:10.1063/1.474578

Cited by 31 publications

(33 citation statements)

References 30 publications

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“…The attracting interaction between the reversed micelles increases with added water-soluble polymer. Similar results were also found by several groups [28,29,30] in the investigation of the effect of PEO and cytochrome C on the microemulsion composed of water, AOT, and isooctane.…”

Section: Conductivities Of the Reversed Micelles In The Presence Of Dsupporting

confidence: 78%

The interaction between poly(vinylpyrrolidone) and reversed micelles of water/AOT/ n -heptane

Luan

Dai

et al. 2003

Colloid & Polymer Science

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Section: Conductivities Of the Reversed Micelles In The Presence Of Dsupporting

confidence: 78%

The interaction between poly(vinylpyrrolidone) and reversed micelles of water/AOT/ n -heptane

Luan

Dai

et al. 2003

Colloid & Polymer Science

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“…In an attempt to understand behavior of a protein in a crowded environment several groups have investigated structural and biochemical activity of www.elsevier.com/locate/cplett many proteins inside the water pool of a reverse micelle using circular dichroism [21], NMR [22] and small angle X-ray and dynamic light scattering [23].…”

Section: Introductionmentioning

confidence: 99%

Solvation dynamics in DMPC vesicle in the presence of a protein

Dutta

Sen

Mukherjee

et al. 2003

Chemical Physics Letters

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“…[6,7] This local environment leads to a conformational transition of cytochrome C from its folded structure to an amphiphilic entity. [8] Hence, the NOESY spectra of cytochrome C in AOT micelles dissolved in pentane, shown in Figure 1c and d, exhibit a very peculiar behavior.…”

Section: Resultsmentioning

confidence: 99%

Novel Zwitterionic Reverse Micelles for Encapsulation of Proteins in Low‐Viscosity Media

Doussin

Birlirakis

Georgin

et al. 2006

Chemistry A European J

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Large proteins remain inaccessible to structural NMR studies because of their unfavorable relaxation properties. Their solubilization in the aqueous core of reverse micelles, in a low-viscosity medium, represents a promising approach, provided that their native tertiary structure is maintained. However, the use of classical ionic surfactants may lead to protein unfolding, due to strong electrostatic interactions between the polar head groups and the protein charges. To design reverse micelles in which these interactions are weakened, a new zwitterionic surfactant molecule was synthesized and studied by high-resolution NMR spectroscopy, for which cytochrome C and 15N-labeled ubiquitin were used as guest candidates. At different ionization states, both proteins are encapsulated in the absence of salts or other additives, in a folded conformation similar to the native one.

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Cytochrome-c in reverse micelles: Small angle x-ray scattering measurements, percolation process, and critical behavior: An interpretation with an association model

Abstract: Articles you may be interested inStructure and dynamics of water in nonionic reverse micelles: A combined time-resolved infrared and small angle x-ray scattering study

Cited by 31 publications

References 30 publications

The interaction between poly(vinylpyrrolidone) and reversed micelles of water/AOT/ n -heptane

The interaction between poly(vinylpyrrolidone) and reversed micelles of water/AOT/ n -heptane

Solvation dynamics in DMPC vesicle in the presence of a protein

Novel Zwitterionic Reverse Micelles for Encapsulation of Proteins in Low‐Viscosity Media

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