Occurrence of chain folding in micelles

Bockstaele, M. Van; Gelan, J.; Martens, H.; Put, J.; Schryver, F. C. De; Dederen, J.G.

doi:10.1016/0009-2614(80)80135-7

Cited by 24 publications

(9 citation statements)

References 20 publications

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“…The chain conformations of the SDS molecules in the micelle and the struct ureof micelles are still subject of controversy {Dill, 1982;Dill etal., 1984;Menger& Doll, 1984). NMR measurements of the relaxation times of the l3C resonances of the SDS chain indicated that chain folding occurs and that the terminal methyl group sometimes touches the surface of the micelle (Van Bockstaele et al, 1980). ESR measurements showed that although the alkyl chain of SDS may be slightly bent, the overall conformation of the chain must be extended (Szajdzinska-Pietik et al, 1985).…”

Section: Resultsmentioning

confidence: 99%

Location of M13 Coat Protein in Sodium Dodecyl Sulfate Micelles As Determined by NMR

Papavoine¹,

Konings²,

Hilbers³

et al. 1994

Biochemistry

119

112

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The major coat protein (gVIIIp) of bacteriophage M13 solubilized in sodium dodecyl sulfate (SDS) detergent micelles was used as a model system to study this protein in the lipid-bound form. In order to probe the position of gVIIIp relative to the SDS micelles, stearate was added, spin-labeled at the 5- or 16-position with a doxyl group containing a stable nitroxide radical. The average position of the spin-labels in the micelles was derived from the line broadening of the resonances in the 13C spectrum of SDS. Subsequently, we derived a model of the relative position of gVIIIp in the SDS micelle from the effect of the spin-labels on the gVIIIp resonances, monitored via 1H-15N HSQC and TOCSY experiments. The results are consistent with the structure of gVIIIp having two helical strands. One strand is a long hydrophobic helix that spans the micelle, and the other is a shorter amphipathic helix on the surface of the micelle. These results are in good agreement with the structure of gVIIIp in membranes proposed by McDonnell et al. on the basis of solid state NMR data [McDonnell, P. A., Shon, K., Kim, Y., & Opella, S. J. (1993) J. Mol. Biol. 233, 447-463]. This study indicates that high-resolution NMR on this membrane protein, solubilized in detergent micelles, is a very suitable technique for mimicking these proteins in their natural environment. Furthermore, the data indicate that the structure of the micelle near the C-terminus of the major coat protein is distorted.(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Resultsmentioning

confidence: 99%

Location of M13 Coat Protein in Sodium Dodecyl Sulfate Micelles As Determined by NMR

Papavoine¹,

Konings²,

Hilbers³

et al. 1994

Biochemistry

119

112

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“…Internal motions in micelles can be studied experimentally using NMR [3][4][5][6] and neutron scattering techniques. [7][8][9][10][11][12][13][14][15] NMR studies in solution show the existence of two kinds of motion: (i) a slow motion with correlation times of the order of nanoseconds arising from the aggregate tumbling and lateral diffusion of the surfactant molecules around the micellar surface and (ii) a faster motion with correlation times of the order of picoseconds which is assigned to bond isomerizations or torsional motions.…”

Section: Introductionmentioning

confidence: 99%

“…25,26 Amphiphilic molecules in micelles exhibit complex dynamical behaviour with a superposition of different motions, which includes segmental motions of the monomers, torsional motions, bond isomerizations, librations, and lateral diffusion on a curved surface, covering a wide time scale from nanoseconds to picoseconds. [3][4][5][6][7][8][9][10][11][12][13][14][15][16]25,26 As previously mentioned, QENS can provide detailed insight into the dynamical behavior and has been used to study a number of micellar systems. [8][9][10][11][12][13][14][15] The type of molecular mode probed depends on the energy resolution and window of the spectrometer used.…”

Section: Introductionmentioning

confidence: 99%

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The dynamical landscape in CTAB micelles

et al. 2012

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“…The spectroscopy of the surfactant molecules (NMR [8][9][10], Raman [11,12] [19,24,25], a sample was synthesized which was selectively deuterated on the 3d carbon after the head group [26]. The intensity and shape of the deuterated carbon's line are drastically modified; thus that line was easily assigned; then the lines of the 4" and Sth carbons were assigned through their isotopic shifts.…”

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confidence: 99%

Structure of the water/surfactant interface in micelles : an NMR study of SDS micelles labelled with paramagnetic ions

Cabane

1981

J. Phys. France

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Résumé. 2014 On présente une méthode nouvelle pour déterminer la structure de l'interface eau/surfactant et la configuration des molécules dans les micelles de surfactant. Cette méthode consiste à observer par RMN les interactions dipolaires entre les noyaux des molécules de surfactant et des contreions paramagnétiques adsorbés sur la surface de ces micelles. L'experience compare les vitesses de relaxation de noyaux appartenant à différents groupes chimiques dans les molécules de surfactant; dans certains cas simples ces vitesses de relaxation dépendent seulement des distances entre les noyaux et les ions. Ainsi les vitesses de relaxation mesurées peuvent être reliées aux populations des noyaux dans des couches situées à diverses profondeurs de la surface. Les résultats mènent à la discuscussion suivante pour la structure de ces couches successives : (i) couches de surface contenant les charges hydratées (sont-elles lisses ou rugueuses ?); (ii) couches de contact eau/hydrocarbone (jusqu'à quelle profondeur l'eau pénètre-t-elle dans la micelle ?); (iii) couches du coeur hydrocarboné (quel est le degré d'organisation des chaines du surfactant ?).Abstract. 2014 A method has been developed for determining the structure of the water/surfactant interface and the configuration of the surfactant molecules in micelles. In this method, NMR is used to measure the magnetic dipolar interactions between the nuclei of the surfactant molecules and paramagnetic counterions adsorbed on the surface of the micelles. The experiment compares the relaxation rates of nuclei belonging to different chemical groups in the surfactant molecules; in some simple cases these relaxation rates only depend on the distances between the nuclei and the ions. Then the measured relaxation rates can be related to the populations of the nuclei in layers located at various depths from the paramagnetic surface. According to the data, the structure of these successive layers in a spherical micelle can be discussed in the following terms : (i) outermost layers containing the hydrated charges (how smooth or regular are they ?) ; (ii) layers of water/hydrocarbon contact (how deep does water penetrate in the micelle ?) ; (iii) layers of the hydrocarbon core (how disorganized is the packing of the surfactant chains ?).J. Physique 42 (1981)

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Occurrence of chain folding in micelles

Cited by 24 publications

References 20 publications

Location of M13 Coat Protein in Sodium Dodecyl Sulfate Micelles As Determined by NMR

Location of M13 Coat Protein in Sodium Dodecyl Sulfate Micelles As Determined by NMR

The dynamical landscape in CTAB micelles

Structure of the water/surfactant interface in micelles : an NMR study of SDS micelles labelled with paramagnetic ions

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