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PubMed2005

Effective interaction of charged platelets in aqueous solution: investigations of colloid laponite suspensions by static light scattering and small-angle x-ray scattering.

We study dilute aqueous solutions of charged disklike mineral particles (laponite) by a combination of static light scattering (SLS) and small-angle x-ray scattering (SAXS). Laponite solutions are known to form gels above a certain critical concentration that must be described as nonequilibrium states. Here we focus on the investigation by SLS and SAXS at concentrations below gelation (c<0.016 g/L) and at low concentrations of added salt (0.001M and 0.005M). Thus, we have obtained the scattering function of single Laponite platelets as well as the structure factor describing their interaction at finite concentration. A detailed analysis of the combined sets of data proves that the solutions are in a well-defined equilibrium state. Moreover, this analysis demonstrates the internal consistency and accuracy of the scattering functions obtained at finite concentrations. We find that laponite particles interact through an effective pair potential that is attractive on short range but repulsive on longer range. This finding demonstrates that Laponite solutions exhibit only a limited stability at the concentration of added salt used herein. Raising the ionic strength to 0.005M already leads to slow flocculation as is evidenced from the enhanced scattering intensity at smallest scattering angles. All data strongly suggest that the gelation occurring at higher concentration is related to aggregation.

Journal Article↗

PubMed1981

Deformation and orientation of red blood cells in a simple shear flow. Theoretical study and approach at small angle light scattering.

On the basis of a simple theoretical model representing the rheological behaviour of the erythrocyte membrane, the authors have proceeded with a theoretical and experimental investigation on the light-scattering diagrams at small angles of normal red blood cells subjected to Couette flow. The results show that the light-scattering diagrams take into account not only cell deformation, but also cell orientation. The prospects for applying this method to the analytical separation of cells with different deformabilities are considered.

Biophysical Phenomena↗

PubMed1989

High-pressure small-angle neutron scattering (SANS) study of 1,2-dielaidoyl-sn-glycero-3-phosphocholine bilayers.

Small-angle neutron scattering of the trans-unsaturated DEPC has been investigated as a function of pressure at 12, 18.6 and 35 degrees C. A pressure-induced structural phase transition from a liquid-crystalline state to a gel state is observed at the temperatures studied. The critical pressure of this transition increases with increasing temperature with a delta P/delta T value of 51 bar/C degrees. The small-angle neutron scattering results indicate that the effect of the trans double bonds in DEPC is to enhance the conformational disorder in the hydrocarbon chains. In DEPC bilayers, a pressure-induced conformational ordering process is observed not only in the liquid-crystalline phase but also in the gel phase, which indicates that conformational disorder exists in the liquid-crystalline phase as well as in the gel phase.

Fatty Acids, Unsaturated↗

PubMed1994

Small angle neutron scattering studies of structural characteristics of agarose gels.

The 30 m small angle neutron scattering facility at the National Institutes of Standards and Technology has been used to examine neutron scattering from agarose gels formed in D2O. Differential scattering cross sections have been acquired over a continuous range of Q between 0.005 and 0.3 A-1. Subtle changes in gel structure are observed when pre-gelation agarose concentration is varied. Similarly, except when the gelling solution is rapidly cooled to a low temperature, the rate at which the gels are formed does not seem to have much effect. Clearer evidence of structural rearrangement is observed when the solvent quality is changed by the addition of dimethyl sulfoxide, or when the temperature of the gel is elevated above 70 degrees C. These data are consistent with a description of a randomly structured polymer network containing discrete self-similar, hydrogen-bonded, junctions normally of minimal thickness approximately 35-40 A.

Carbohydrate Conformation↗

PubMed1993

Small angle neutron scattering studies of C8 and C9 and their interactions in solution.

Small angle neutron scattering (SANS) results revealed that contrary to most reports C9 is not a globular protein. Its radius of gyration (Rg) at pH 8 and an ionic strength of 0.5 is 32.2 +/- 1.4 A increasing to 35 A at physiologic ionic strength. In contrast, C8, which has a 2.2-fold larger mass, has a similar Rg value [34.6 +/- 1.6 A]. Calibration plots of Rg vs. M(r) indicate that native C8 is a spherical protein whereas native C9 is elongated. From previous reports it was known that native C8 and C9 associate in solutions of low ionic strength. SANS results confirmed this observation but also demonstrated that C8-C9 heterodimers are already formed at physiologic ionic strength. The dimeric complex is globular [Rg = 40 +/- 0.8 A] indicating that the proteins associate side-by-side rather than end-to-end. In contrast, in presence of the drug Suramin, a potent inhibitor of the assembly of the C5b-9 complex, C9 forms a complex with twice the molecular mass that is still elongated (Rg = 48.8 +/- 0.8 A), suggesting that in this case the protein dimerizes end-to-end via a bridging Suramin molecule.

Biophysical Phenomena↗

PubMed2004

Detailed modeling of the volume fraction profile of adsorbed polymer layers using small-angle neutron scattering.

A detailed analysis of on and off-contrast small-angle neutron scattering from poly(ethylene oxide)s adsorbed on polystyrene latex is presented. The results have been fitted to an exponential decay, self-consistent mean-field (SCF) and scaling models of the volume fraction profile. As the chain length increases a clear self-similar layer emerges in both the SCF and scaling profiles. The RMS thickness of the adsorbed layer in the plateau of the adsorption isotherm varies as M0.4 for both the SCF and scaling profiles but the exponential one however gives a much lower exponent consistent with the neglect of the tail or distal region. The new constrained version of the Scheutjens-Fleer model was able to predict the structure of the layer and hence the scattering with great accuracy.

Journal Article↗

PubMed2005

Small-angle neutron scattering studies of charged carboxyl-terminated dendrimers in solutions.

Small-angle neutron scattering was used to characterize the solution behavior of charged carboxylic acid terminated "cascade" dendrimers (Z-Cascade/methane [4]/3-oxo-6-oxa-2-azaheptylidyne/3-oxo-2-azaheptylidyne/propanoic acids) of third (G3) and fifth (G5) generations as a function of dendrimer concentration, pH, and ionic strength. An increase in dendrimer concentration leads to a single broad peak in the scattering profile arising from interdendrimer interaction. The dissociation of terminal carboxylate groups also gives rise to an interdendrimer interaction peak, which could be suppressed by the addition of excess salt. The results of contrast matching measurements indicate the accumulation of an excess concentration of tetramethylammonium counterions around the surface of these highly charged particles, and the thickness of these counterions lies somewhere between 4 and 6 A. This conclusion is consistent with our previous potentiometric titration (Zhang, H.; et al. J. Phys. Chem. B 1997, 101, 3494) and capillary electrophoresis (Huang, Q. R.; et al. J. Phys. Chem. B 2000, 104, 898) data.

Journal Article↗

PubMed1996

Small angle neutron scattering from lysozyme solutions in unsaturated and supersaturated states (SANS from lysozyme solutions).

Small angle neutron scattering (SANS) method was used to study lysozyme solutions, with particular interest in an understanding of the crystallization process at the initial stage. It is found that (1) in the unsaturated solution, the protein molecules aggregate with a continuous increase in size when NaCl concentration is increased, and (2) in the supersaturated solution, an irreversible change, superimposed on the former process, occurs when the supersaturation is realized. These facts indicate the usefulness of SANS in detecting changes of protein molecules in solution on the nanometer scale. The reliability of the SANS results are indicated by (1) comparing them with those of small angle X-ray scattering (SAXS), and (2) comparing the effect of D(2)O and H(2)O as solvent. Since the interparticle interaction is essential in the crystallization process and a simple Guinier plot analysis is not allowed, a more rigorous framework of analyzing data with interference function is developed, through which both average interparticle distance and particle size are estimated.

Journal Article↗

PubMed1981

Small-angle neutron scattering studies of the conformation of myeloma protein MOPC315 and its Fab fragment, and the interaction with a monovalent dinitrophenyl hapten.

The first small-angle scattering study of an immunoglobulin A is reported. Neutron measurements have been made to determine conformational parameters of the mouse myeloma protein MOPC315 and to relate these to previous immunoglobulin G results. Use of the contrast method shows that the MOPC315 IgA molecule is not simply globular, that it has a dry volume of 220.0 +/- 4.5 nm3 corresponding to a mass density of 1.275 +/- 0.025 g cm-3 and that its full and cross-sectional radii of gyration, corrected for concentration dependence, are 7.97 +/- 0.07 nm, 2.40 +/- 0.08 nm and 1.33 +/- 0.07 nm respectively. Similar study of its Fab fragment gives a dry molecular volume of 69.0 +/- 0.7 nm3, a mass density of 1.285 +/- 0.015 g cm-3 and uncorrected radii of gyration that are consistent with those of the parent and support an overall "T" or "Y" conformation in solution. Addition to saturation of a small monovalent dinitrophenyl hapten leaves the dry volume of the whole molecule unaltered, but may slightly lower one or more of its radii of gyration. The significance of this finding is discussed. Comparative studies with rabbit anti-dinitrophenyl immunoglobulin G antibody suggest a different initial conformation but similar consequences of hapten binding, which, if real, are probably unrelated to classical complement fixation.

Amino Acid Sequence↗

PubMed1988

Phycocyanin aggregation. A small angle neutron scattering and size exclusion chromatographic study.

The influence of environmental factors on the aggregation properties of phycocyanin from Synechocystis 6701 was studied by small angle neutron scattering and high-pressure size-exclusion liquid chromatography. Phycocyanin was found to exist in a reversible equilibrium between the monomer, trimer and hexamer forms. The distribution of the protein between these oligomers is determined by the pH, buffer composition and ionic strength of the medium, and protein concentration. Phycocyanin was in a stable hexameric state at pH 5.0 to 6.0 at a concentration of 1 to 10 mg/ml, and was primarily in a trimeric state at pH 8.0 at a concentration of about 5 mg/ml. Comparison of the small angle scattering data with the computed scattering curve for a hollow cylinder was used to determine the dimensions of the best-fit model by a least-squares fitting procedure. The outer radius, inner radius and height of the phycocyanin hexamer were found to be 54.1, 12.0 and 61.4 A (1 A = 0.1 nm), respectively, and the corresponding dimensions for the trimer were 54.5, 14.0 and 33.0 A. The molecular weight ratio for phycocyanin hexamer was determined to be 217,000. The dimensions and molecular weight ratios of phycocyanin from Synechocystis 6701 obtained by solution scattering are similar to the values for Mastigocladus laminosus obtained by X-ray crystallography.

Chromatography, High Pressure Liquid↗

PubMed1992

Structure of RecA-DNA complexes studied by combination of linear dichroism and small-angle neutron scattering measurements on flow-oriented samples.

By combining anisotropy of small-angle neutron scattering (SANS) and optical anisotropy (linear dichroism, l.d.) on flow-oriented RecA-DNA complexes, the average DNA-base orientation has been determined in RecA complexes with double-stranded (ds) as well as single-stranded (ss) DNA. From the anisotropy of the two-dimensional SANS intensity representation, the second moment orientation function S is obtained. Knowledge of S is crucial for the interpretation of l.d. spectra in terms of orientation of the DNA bases and the aromatic amino acid residues. The DNA-base planes are essentially perpendicular to the fibre axis of the complex between RecA and dsDNA in the presence of cofactor ATP gamma S. A somewhat tilted base geometry is found for the RecA-ATP gamma S complexes with single-stranded poly(dT) and poly(d epsilon A). This behaviour contrasts the RecA-ssDNA complex formed without cofactor which displays a poor orientation of the bases. Well-ordered bases in the ssDNA-RecA complex is possibly reflecting the role of RecA in preparing a nucleotide strand for base-pairing in the search-for-homology process. While the central SANS intensity is essentially independent of the pitch of the helical complex, a secondary intensity maximum, which becomes focused upon flow orientation, is found to be a sensitive measure of the pitch. The pitch values for the complexes compare well with cryo-electron microscopy results but are slightly larger than those seen for uranyl-stained samples.

Adenosine Triphosphate↗

PubMed1997

Small-angle neutron scattering by a strongly denatured protein: analysis using random polymer theory.

Small-angle neutron scattering profiles are presented from phosphoglycerate kinase, in the native form and strongly denatured in 4 M guanidinium chloride (GdnHCl) solution. The data are interpreted using a model in which the excess scattering density associated with the protein is represented as a finite freely jointed chain of spheres. The similarity of the model-derived scattering function to experiment increases asymptotically with the number of spheres. The improvement of the fit obtained with more than approximately 200 spheres (i.e., two residues per sphere) is insignificant. The effects of finite size of the scattering units and of scattering length variation along the polypeptide chain are examined. Improved agreement with experiment is obtained when these effects are taken into account. A method for rapid calculation of the scattering profile of a full, all-atom configuration is examined. It is found that a representation of the chain containing two scattering units per residue, placed at the backbone and side-chain scattering length centroids, reproduces the full, all-atom profile to within 2%.

Fourier Analysis↗

PubMed2005

A coarse graining approach to determine nucleic acid structures from small angle neutron scattering profiles in solution.

We present a theoretical method to calculate the small angle neutron scattering profile of nucleic acid structures in solution. Our approach is sensitive to the sequence and the structure of the nucleic acid. In order to test our approach, we apply this method to the calculation of the experimental scattered intensity of the decamer d(CCAACGTTGG)2 in H2O. This sequence was specifically chosen for this study as it is believed to adopt a canonical B-form structure in 0.3 M NaCl. We find that not only will our methodology reproduce the experimental scattered intensity for this sequence, but our method will also discriminate between B-, A- and Z-form DNA. By studying the scattering profile of this structure in 0.5 and 1.0 M NaCl, we are also able to identify tetraplex and other similar oligomers formation and to model the complex using the experimental scattering data in conjunction with our methodology.

Base Sequence↗

PubMed2003

Small-angle neutron scattering studies of aqueous solutions of short-chain amphiphiles.

We present small angle neutron scattering measurements on binary aqueous solutions of some short-chain amphiphiles (diols, triols, glycols and diglycols) at room temperature. The spectra were analysed in terms of the Teubner-Strey phenomenological formula which allows to obtain a measure for the amphiphilicity strength of each system (amphiphilicity factor fa). In some systems, however, other models, valid for micellar solutions, give also a good representation of the spectra. As a result, we find that, independently of the type of hydrophilic group side (oxydrilic or oxirane), these systems cover the entire accessible amphiphilicity scale ( -1 < fa < 1). Some disordered systems (fa > 1) presumably are able to form micelle-like aggregates.

Journal Article↗

PubMed1996

Investigation of the structure of thylakoid membranes (spinach) by means of small-angle neutron scattering.

This paper presents experimental data on the determination of the thickness of thylakoid membranes by small-angle neutron scattering. The thylakoids were isolated from spinach chloroplasts. The partial volume of proteins and lipids in the "washed" and "unwashed" membranes was estimated. It is shown that the thickness of thylakoid membranes, measured with this techniques depends on the way the membranes were separated. When isolated thylakoids by the standard method, the membrane thickness amounted to 75 A but if the extracted thylakoids were additionally washed with the isolation medium, the measured thickness was 50 A. In this case a significant decrease in the protein partial volume of the membrane was observed. The obtained results make it possible to explain numerous data on X-ray and small-angle neutron scattering by thylakoid membranes of different origins, proceeding from the assumption that all these membranes have a unified structure and consist of a stable core with a thickness of about 50 A, and layers of peripheral, weakly bound proteins with a thickness which may depends on the nature of the object under investigation and extracting conditions.

Chloroplasts↗

PubMed2005

An in situ study of the t-butyllithium initiated polymerization of butadiene in d-heptane via small angle neutron scattering and 1H-NMR.

We present a combined 1H-NMR and small angle neutron scattering in situ study of the anionic polymerization of butadiene using t-butyllithium as the initiator. Both initiation and propagation phases were explored. This combined approach allows the structural and kinetic characteristics to be accessed and cross compared. The use of the D22 instrument (ILL Grenoble) permits the attainment of Q approximately equal to 2 x 10(-3) A. This, in turn, led to the identification of coexisting large-scale and smaller aggregates during all stages of the polymerization. The smaller aggregates contain most of the reacted monomers. Their structure changes from high functionality wormlike chains at early stages of the reaction to starlike aggregates where the crossover occurs at a degree of polymerization of approximately equal to 40. The initiation event involved these small, high functionality (approximately equal to 120) aggregates that apparently consisted of cross-associated t-butyllithium with the newly formed allylic-lithium head groups. As the initiation event progressed the initiation rate increased while the functionality of these small aggregates decreased and their size increased. Propagation, in the absence of initiation, was found to have a rate constant that was molecular weight dependent. At approximately 11 kg/mol the measured polymerization rate was found to increase while no further structural changes were seen.

Journal Article↗

PubMed1981

Small-angle neutron scattering study of lipid phase diagrams by the contrast variation method.

A small-angle neutron scattering (SANS) study of slightly sonicated liposomes of binary lipid mixtures is presented. It is demonstrated that the neutron scattering of lipid lamellae may be analyzed in terms of the Kratky--Porod model of scattering by two-dimensional systems. The contrast variation technique may thus be applied in order to study the structure and phase diagrams of lipid layers not disturbed by heavy sonication. The thickness of isolated bilayers is measured, and molar volumes of pure lipid phases are determined. Mixtures of deuterated dimyristoylphosphatidylcholine with (1) protonated dipalmitoylphosphatidylcholine and (2) protonated distearoylphosphatidylcholine, respectively, are studied. Excess volumes of lipid mixtures are determined by the contrast variation. For the first mixture positive excess volumes of +86 A3 in the crystalline phase (5 degrees C) and of +49 A3 in the fluid phase (35 degrees C) are obtained. These large positive excess volumes are interpreted in terms of free volume creation at the interface between the monolayers, which indicates that the polar head groups are rather fixed with respect to the lipid--water interface. We show that the phase boundaries at a given temperature may be determined by performing contrast variation experiments for two mixtures with different initial composition. Good agreement with existing experimental data is observed for the first mixture. A miscibility gap is established in the crystalline state of the second mixture. A most interesting result is the finding of an immiscibility in the fluid state. This is interpreted in terms of critical concentration fluctuations caused by the critical demixing point of the solid-state miscibility gap hidden below the liquidus line.

Deuterium↗

PubMed2000

Small-angle neutron scattering from large unilamellar vesicles: an improved method for membrane thickness determination.

Small-angle neutron scattering (SANS) measurements were performed on large unilamellar vesicles (LUVs) in order to investigate solute effects on membrane properties. Although SANS is a well established technique for the measurement of membrane thickness in unilamellar vesicles, earlier measurements have depended on approximate treatments of the scattering function and have suffered from effects of multilamellarity or difficulty in sample preparation. More recent studies of temperature induced thickness changes in DPPC LUVs which have included explicit treatment of the full scattering function were complicated by disparities between the predicted and measured scattering curves. Here, we reexamine theoretical descriptions of SANS from LUVs. Motivated by our observations, we then introduce a new method for interpretation of SANS data, which we compare to established techniques and apply to our measurements.

Lipid Bilayers↗