Structure of ionic micelles from small angle neutron scattering

Bendedouch, Dalila; Chen, Sow Hsin; Koehler, W. C.

doi:10.1021/j100224a033

Cited by 136 publications

(99 citation statements)

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“…The increase in SDS micelle size and aggregation number, and change in micelle shape upon surfactant addition that is observed here are consistent with what has been reported in the literature [37][38][39][40][41][42][43][44]47,50,51]. Similarly, stronger interactions, higher total micelle charge, and reduction in isothermal compressibility with increasing surfactant concentration have also been reported in the literature [52].…”

Section: Tablesupporting

confidence: 94%

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Self-assembly control via molecular recognition: Effect of cyclodextrins on surfactant micelle structure and interactions determined by SANS

Fajalia

Tsianou

2015

Colloids and Surfaces A: Physicochemical and Engineering Aspect

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Section: Tablesupporting

confidence: 94%

“…SANS has been utilized to characterize SDS micelles in aqueous solutions, in the absence or presence of salt with different counterions [37][38][39][40][41][42][43][44]. However, SANS investigations of SDS in the presence of CDs have not been previously reported.…”

Section: Introductionmentioning

confidence: 99%

Self-assembly control via molecular recognition: Effect of cyclodextrins on surfactant micelle structure and interactions determined by SANS

Fajalia

Tsianou

2015

Colloids and Surfaces A: Physicochemical and Engineering Aspect

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“…Please note that SDS micelle has been selected as a model system because it is the most intensively-characterized micelle through experimental analysis [17][18][19][20][21][22][23][24][25][26][27][28][29][30][31][32][33] and simulation methods [34][35][36][37][38][39][40][41][42][43][44][45]. In experimental approaches, various techniques such as light scattering [18][19][20][21], fluorescence [24,25], SAXS [17,31] and SANS [23,26,27] have been used to characterize the size, shape, aggregation and charge of the SDS micelle at various conditions for concentration and temperature. Here it is noted that, despite great development in such experimental analysis, it is still challenging to attain molecular-level information of the internal structure of the SDS micelle experimentally.…”

Section: Introductionmentioning

confidence: 99%

Molecular dynamics simulation study of sodium dodecyl sulfate micelle: Water penetration and sodium dodecyl sulfate dissociation

Chun

Choi

Jang

2015

Colloids and Surfaces A: Physicochemical and Engineering Aspect

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h i g h l i g h t s• SDS micelle was simulated for 20 ns using all-atom MD simulation.• SDS conformations are mostly bent in micelle.• Free volume in SDS micelle is ∼0.35% of the micelle volume.• Free energy change for water penetration through SDS micelle is ∼10 kcal/mol.• Dissociation of a single SDS molecule from the micelle requires ∼13 kcal/mol. g r a p h i c a l a b s t r a c t a b s t r a c tWe investigate a micelle consisting of 60 sodium dodecyl sulfate (SDS) molecules in water phase using molecular dynamics simulation method. The dimension of the micelle is evaluated as ∼16Å and ∼21Å for the radius of gyration and geometric radius, respectively, which are well agreed with the previous studies. By calculating the formation energy, it is found that the stability of micelle is driven by the interaction of the micelle with water phase. Via Connolly surface analysis, it was found that ∼58% of the micelle surface is occupied by the hydrophobic alkyl tails. The conformation analysis shows that the individual SDS molecules are bent within the micelle and are not aligned radially from the center-of-mass of the micelle. However, it turns out that the micelle is well packed with a small free volume (0.35% of the micelle volume) which does not allow the diffusion-in of water molecules. The PMF required to drag a water molecule from water phase to the center-of-mass of micelle is calculated as ∼10 kcal/mol while the PMF for a SDS molecule to be dissociated from the micelle is ∼13 kcal/mol, both of which demonstrate that the micellization is driven by minimizing unfavorable interaction of hydrophobic alkyl tail of SDS molecule with water phase.

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“…The SAXS profile of a protein dispersed in aqueous solution with no interaction (or interference) can be described by IðQÞ ¼ I 0P PðQÞ, whereP PðQÞ is the normalized form factor, withP Pð0Þ ¼ 1 (Bendedouch et al, 1983;Chen, 1986), and the modulus of scattering vector Q ¼ ð4=Þ sin , where the scattering angle is 2 and the wavelength is . The zero scattering intensity I 0 ¼ CNðf À s V dry Þ 2 is determined by the concentration C, aggregation number N (for non-aggregated proteins N = 1), dry volume of protein V dry , scattering length f of the protein, and the scattering-length density s of the solvent (Chen & Lin, 1987;Wu & Chen, 1988;Feigin & Svergun, 1987).…”

Section: Saxs Modelmentioning

confidence: 99%

A modified Ising model for the thermodynamic properties of local and global protein folding–unfolding observed by circular dichroism and small-angle X-ray scattering

Shiu

Jeng

et al. 2007

J Appl Cryst

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Based on the mean‐field approximation, we have applied a modified Ising model to describe general protein unfolding behavior at thermodynamic equilibrium with the free energy contributed by the subgroup units (amino acids or peptide bonds) of the protein. With the thermodynamic properties of the protein, this model can associate the stepwise change of an unfolding fraction ratio profile with the local and global conformation unfolding. Taking cytochrome c (cyt c) as a model protein, we have observed, using small‐angle X‐ray scattering and circular dichroism (CD), the global and local structure changes for the protein in three kinds of denaturant environments: acid, urea and guanidine hydrochloride. The small‐angle X‐ray scattering and CD results are mapped to the unfolding fractions as a function of the pH value or denaturant concentration, from which we have extracted local and global unfolding free energies of cyt c in different denaturant environments using a modified Ising model. Based on the characteristics of the thermodynamic properties deduced from the local and global protein folding–unfolding, we discuss the thermodynamic stabilities of the protein in the three denaturant environments, and the possible correlation between the global conformation change of the protein and the local unfolding activities of the S—Fe bond in the Met80‐heme and the α‐helices.

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Structure of ionic micelles from small angle neutron scattering

Cited by 136 publications

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Self-assembly control via molecular recognition: Effect of cyclodextrins on surfactant micelle structure and interactions determined by SANS

Self-assembly control via molecular recognition: Effect of cyclodextrins on surfactant micelle structure and interactions determined by SANS

Molecular dynamics simulation study of sodium dodecyl sulfate micelle: Water penetration and sodium dodecyl sulfate dissociation

A modified Ising model for the thermodynamic properties of local and global protein folding–unfolding observed by circular dichroism and small-angle X-ray scattering

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