Resolution effects and analysis of small-angle neutron scattering data

Pedersen, Jan Skov

doi:10.1051/jp4:19938102

Cited by 58 publications

(76 citation statements)

References 7 publications

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“…The p(r) function is approximated by a sum of cubic spline functions, which are defined in the range 0 Յ r Յ D max . The Fourier transform of p(r) smeared by instrumental smearing 42,43 is fitted to the measured data by a leastsquares procedure with a smoothness constraint. We used the smallest value of D max that gives a smooth solution for p(r).…”

Section: Indirect Fourier Transformation Of Sans Datamentioning

confidence: 99%

Association behavior of native ?-lactoglobulin

Verheul¹,

Pedersen

Roefs³

et al. 1999

Biopolymers

196

173

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Section: Indirect Fourier Transformation Of Sans Datamentioning

confidence: 99%

Association behavior of native ?-lactoglobulin

Verheul¹,

Pedersen

Roefs³

et al. 1999

Biopolymers

196

173

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“…Various theoretical models of particle-polymer mixtures have been utilized in previous work, aiming to quantify the various interactions and to establish how they affect the macroscopic properties [5][6][7][8][9][10][11] . Several experimental methods are available to elucidate the structure of particlepolymer mixtures, which can then be compared with the model predictions [12][13][14][15][16][17][18][19][20] . Most of them are based on some form of scattering, with light or neutrons.…”

Section: Introductionmentioning

confidence: 99%

Theoretical predictions of structures in dispersions containing charged colloidal particles and non-adsorbing polymers

Xie

Turesson

Woodward

et al. 2016

Phys. Chem. Chem. Phys.

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We develop a theoretical model to describe structural effects on a specific system of charged colloidal polystyrene particles, upon the addition of non-adsorbing PEG polymers. This system has previously been investigated experimentally, by scattering methods, so we are able to quantitatively compare predicted structure factors with corresponding experimental data. Our aim is to construct a model that is coarse-grained enough to be computationally manageable, yet detailed enough to capture the important physics. To this end, we utilize classical polymer density functional theory, wherein all possible polymer configurations are accounted for, subject to a mean-field Boltzmann weight. We make efforts to counteract drawbacks with this mean-field approach, resulting in structural predictions that agree very well with computationally more demanding simulations. Electrostatic interactions are handled at the fully non-linear Poisson-Boltzmann level, and we demonstrate that a linearization leads to less accurate predictions. The particle charge is an experimentally unknown parameter. We define the surface charge such that the experimental and theoretical gel point at equal polymer concentration coincide. Assuming a fixed surface charge for a certain salt concentration, we find very good agreement between measured and predicted structure factors across a wide range of polymer concentrations. We also present predictions for other structural quantities, such as radial distribution functions, and cluster size distributions. Finally, we demonstrate that our model predicts the occurrence of

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“…Throughout the data analysis corrections were made for instrumental smearing. 34,35 For each instrumental setting the ideal scattering curves were smeared by the appropriate resolution function when the model scattering intensity was compared to the measured l(q) by means of leastsquares methods. 36 The resulting fit yields good agreement with the data over the entire q range as shown in Figure 4A and supported by 2 ϭ 2.6.…”

mentioning

confidence: 99%

Size and shape of the repetitive domain of high molecular weight wheat gluten proteins. I. Small‐angle neutron scattering

et al. 2003

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The solution structure of the central repetitive domain of high molecular weight (HMW) wheat gluten proteins has been investigated for a range of concentrations and temperatures using mainly small-angle neutron scattering. A representative part of the repetitive domain (dB1) was studied as well as an "oligomer" basically consisting of four dB1 units, which has a length similar to the complete central domain. The scattering data over the entire angular range of both proteins are in quantitative agreement with a structural model based on a worm-like chain, a model frequently used in polymer theory. This model describes the "supersecondary structure" of dB1 and dB4 as a semiflexible cylinder with a length of about 235 and 900 A, respectively, and a cross-sectional diameter of about 15 A. The flexibility of both proteins is characterized by a persistence length of about 13 A. Their structures are thus quantitatively identical, which implies that the central HMW domain can be elongated while retaining its structural characteristics. It seems conceivable that the flexible cylinder results from a helical structure, which resembles the beta-spiral observed in earlier studies on gluten proteins and elastin. However, compared to the previously proposed structure of a (stiff) rod, our experiments clearly indicate flexibility of the cylinder.

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Resolution effects and analysis of small-angle neutron scattering data

Cited by 58 publications

References 7 publications

Association behavior of native ?-lactoglobulin

Association behavior of native ?-lactoglobulin

Theoretical predictions of structures in dispersions containing charged colloidal particles and non-adsorbing polymers

Size and shape of the repetitive domain of high molecular weight wheat gluten proteins. I. Small‐angle neutron scattering

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