Distance distribution function of sodium dodecyl sulfate micelles by x-ray scattering

Itri, Rosângela; Amáral, L. Q.

doi:10.1021/j100154a074

Cited by 96 publications

(117 citation statements)

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“…micelle of 5 -6.5 nni. Although previously reported analyses, which assume a sharp boundary between the head group region and the core, gave widely varying dimensions (Reiss-Husson and Luzzati, 1966;Kratky and Muller, 1982;Itri and Amaral, 1991), they all fall within the limits set by our simple two shell model. Our results are, however, more consistent with a model of a spherical micelle that has a diffuse boundary between head group and core regions.…”

Section: Structure Of the Sds/micellesupporting

confidence: 73%

Evidence for Sodium Dodecyl Sulfate/Protein Complexes Adopting a Necklace Structure

Samsó

Daban

Hansen³

et al. 1995

European Journal of Biochemistry

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Structural analysis by cryo-electron microscopy and small-angle X-ray scattering of ten sodium dodecyl sulfate/protein complexes in 25 mM Tris/HCI, 0.192 M glycine, pH 8.3, showed necklace-like structures of spherical micelles dispersed along the unfolded peptide chain. The micelles of most SDS/protein complexes had a constant diameter (= 6.2 nm), slightly larger than pure SDS micelles (-5.7 nm), all micelles possessing a degree of surface roughness. The micelle-associated polypeptide is mostly situated at the interface of the sulfate head groups and hydrocarbon core, intruding into the core rather than outward from the surface. Proteins with a molecular mass less than about 20 kDa formed complexes with a single SDS micelle. Multi-micellar SDSIprotein complexes had centre-to-centre intermicellar distances in the range 7.0-12.0 nm. Our findings on the constancy of micellar size, number of micelles/complex, and the relationship between the degree of occupancy of micelles and a polypeptide's molecular mass, have enabled us to speculate on the correlation between the electrophoretic mobility of a polypeptide in SDS/PAGE and its molecular mass. The anomalous electrophoretic behaviour observed for the sodium dodecyl sulfate/histone H5 complex is accounted for by the large micelle of its complex.

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Section: Structure Of the Sds/micellesupporting

confidence: 73%

Evidence for Sodium Dodecyl Sulfate/Protein Complexes Adopting a Necklace Structure

Samsó

Daban

Hansen³

et al. 1995

European Journal of Biochemistry

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“…[13] This model was confirmed by techniques based on electron paramagnetic resonance (EPR). [16] It has been postulated that the small size of the micelles (typical diameter 5 nm [17] ) used in these studies may have artificially constrained the protein into a horseshoe structure, and subsequent studies were performed on small unilamellar vesicles (SUVs) and bicelles. Of the eight studies published on this issue to date, three support the horseshoe [18][19][20] conformation, and five the extended [5,[21][22][23][24] conformation, despite using similar experimental techniques and often with only slight variations in experimental conditions.…”

mentioning

confidence: 99%

Direct Evidence of Coexisting Horseshoe and Extended Helix Conformations of Membrane‐Bound Alpha‐Synuclein

et al. 2010

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Good luck! The physiologically relevant conformation of membrane‐bound α‐Synuclein (αS) can be either a horseshoe or an extended helix structure. Experimental data obtained by site‐directed spin labeling in combination with pulsed electron paramagnetic resonance provide compelling evidence of the coexistence of the horseshoe structure and an extended helix of αS bound to a membrane surface, and potentially resolve the debate on the structure of membrane‐bound αS.

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“…Bruce et al publish 2.20 nm; [11] Itri and Amaral determined R mic 2.23 nm from X-ray scattering; [30] 2.19 nm are obtained by adding 0.468 nm [33] for the headgroup diameter to the core radius reported by Bockstahl and Dupla √tre, R c 1.75 nm). [32] As for R, there is good agreement between the DRS result and the other approaches quoted above, all claiming that SDS micelles are nearly spherical in the investigated concentration range.…”

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confidence: 99%

Micelle and Solvent Relaxation in Aqueous Sodium Dodecylsulfate Solutions

et al. 2003

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Dielectric spectra have been measured for aqueous sodium dodecylsulfate (SDS) solutions up to 0.1 mol L-1 at 25 degrees C over the frequency range 0.005 < or = nu GHz-1 < or = 89. The spectra exhibit two relaxation processes at approximately 0.03 GHz and 0.2 GHz associated with the presence of micelles in addition to the dominant solvent relaxation process at approximately 18 GHz and a small contribution at approximately 1.8 GHz due to H2O molecules hydrating the micelles. Detailed analysis reveals that the micelles bind 20 water molecules per SDS unit, but not as strongly as trimethylalkylammonium halide surfactants do. The relaxation times and amplitudes of both micelle relaxation processes can be simultaneously analysed with the theory of Grosse, yielding the effective volume of a SDS unit in the micelle and the lateral diffusion coefficient of the bound counterions. The findings of this investigation fully corroborate recent molecular dynamics simulations on structure and dynamics of SDS micelles.

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Distance distribution function of sodium dodecyl sulfate micelles by x-ray scattering

Cited by 96 publications

References 0 publications

Evidence for Sodium Dodecyl Sulfate/Protein Complexes Adopting a Necklace Structure

Evidence for Sodium Dodecyl Sulfate/Protein Complexes Adopting a Necklace Structure

Direct Evidence of Coexisting Horseshoe and Extended Helix Conformations of Membrane‐Bound Alpha‐Synuclein

Micelle and Solvent Relaxation in Aqueous Sodium Dodecylsulfate Solutions

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