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      Studying Soft-matter and Biological Systems over a Wide Length-scale from Nanometer and Micrometer Sizes at the Small-angle Neutron Diffractometer KWS-2

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          Abstract

          The KWS-2 SANS diffractometer is dedicated to the investigation of soft matter and biophysical systems covering a wide length scale, from nm to µm. The instrument is optimized for the exploration of the wide momentum transfer Q range between 1x10 -4 and 0.5 Å -1 by combining classical pinhole, focusing (with lenses), and time-of-flight (with chopper) methods, while simultaneously providing high-neutron intensities with an adjustable resolution. Because of its ability to adjust the intensity and the resolution within wide limits during the experiment, combined with the possibility to equip specific sample environments and ancillary devices, the KWS-2 shows a high versatility in addressing the broad range of structural and morphological studies in the field. Equilibrium structures can be studied in static measurements, while dynamic and kinetic processes can be investigated over time scales between minutes to tens of milliseconds with time-resolved approaches. Typical systems that are investigated with the KWS-2 cover the range from complex, hierarchical systems that exhibit multiple structural levels ( e.g., gels, networks, or macro-aggregates) to small and poorly-scattering systems ( e.g., single polymers or proteins in solution). The recent upgrade of the detection system, which enables the detection of count rates in the MHz range, opens new opportunities to study even very small biological morphologies in buffer solution with weak scattering signals close to the buffer scattering level at high Q.

          In this paper, we provide a protocol to investigate samples with characteristic size levels spanning a wide length scale and exhibiting ordering in the mesoscale structure using KWS-2. We present in detail how to use the multiple working modes that are offered by the instrument and the level of performance that is achieved.

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          Analysis of small-angle scattering data from colloids and polymer solutions: modeling and least-squares fitting

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            Monomeric Amyloid Beta Peptide in Hexafluoroisopropanol Detected by Small Angle Neutron Scattering

            Small proteins like amyloid beta (Aβ) monomers are related to neurodegenerative disorders by aggregation to insoluble fibrils. Small angle neutron scattering (SANS) is a nondestructive method to observe the aggregation process in solution. We show that SANS is able to resolve monomers of small molecular weight like Aβ for aggregation studies. We examine Aβ monomers after prolonged storing in d-hexafluoroisopropanol (dHFIP) by using SANS and dynamic light scattering (DLS). We determined the radius of gyration from SANS as 1.0±0.1 nm for Aβ1–40 and 1.6±0.1 nm for Aβ1–42 in agreement with 3D NMR structures in similar solvents suggesting a solvent surface layer with 5% increased density. After initial dissolution in dHFIP Aβ aggregates sediment with a major component of pure monomers showing a hydrodynamic radius of 1.8±0.3 nm for Aβ1–40 and 3.2±0.4 nm for Aβ1–42 including a surface layer of dHFIP solvent molecules.
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              D33—a third small-angle neutron scattering instrument at the Institut Laue Langevin

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                Author and article information

                Journal
                J Vis Exp
                J Vis Exp
                JoVE
                Journal of Visualized Experiments : JoVE
                MyJove Corporation
                1940-087X
                2016
                8 December 2016
                8 December 2016
                : 118
                : 54639
                Affiliations
                1Jülich Centre for Neutron Science Outstation at MLZ, Forschungszentrum Jülich GmbH
                2Department of Chemistry, Louisiana State University
                3Jülich Centre for Neutron Science JCNS-1 & Institute of Complex Systems ICS-1, Forschungszentrum Jülich GmbH
                4Central Institute of Engineering, Electronics and Analytics — Electronic Systems (ZEA-2), Forschungszentrum Jülich GmbH
                5Central Institute of Engineering, Electronics and Analytics — Engineering and Technology (ZEA-1), Forschungszentrum Jülich GmbH
                Author notes

                Correspondence to: Aurel Radulescu at a.radulescu@ 123456fz-juelich.de

                Article
                54639
                10.3791/54639
                5226371
                28060296
                f130fbc3-3aa0-4e26-87a7-70ad08fa0ffb
                Copyright © 2016, Journal of Visualized Experiments

                This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-nd/3.0/

                History
                Categories
                Bioengineering

                Uncategorized
                bioengineering,issue 118,small-angle neutron scattering (sans),high-resolution sans,high-intensity sans,focusing sans,soft matter systems,biophysical systems

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