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- Arzbacher, S., et al.
(författare)
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Tomography based numerical simulation of the demagnetizing field in soft magnetic composites
- 2015
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Ingår i: Journal of Applied Physics. - : AIP Publishing. - 0021-8979 .- 1089-7550. ; 117:16
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Tidskriftsartikel (refereegranskat)abstract
- The magneto-static behaviour of soft magnetic composites (SMCs) is investigated using tomography based direct numerical simulation. The microgeometry crucially affects the magnetic properties of the composite since a geometry dependent demagnetizing field is established inside the composite, which lowers the magnetic permeability. We determine the magnetic field information inside the SMC using direct numerical simulation of the magnetic field based on high resolution micro-computed tomography data of the SMC's microstructure as well as artificially generated data made of statistically homogeneous systems of identical fully penetrable spheres and prolate spheroids. Quasi-static electromagnetic behaviour and linear material response are assumed. The 3D magnetostatic Maxwell equations are solved using Whitney finite elements. Simulations show that clustering and percolation behaviour determine the demagnetizing factor of SMCs rather than the particle shape. The demagnetizing factor correlates with the slope of a 2-point probability function at its origin, which is related to the specific surface area of the SMC. Comparison with experimental results indicates that the relatively low permeability of SMCs cannot be explained by demagnetizing effects alone and suggests that the permeability of SMC particles has to be orders of magnitude smaller than the bulk permeability of the particle material.
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- Manzoni, Francesco, et al.
(författare)
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Elucidation of Hydrogen Bonding Patterns in Ligand-Free, Lactose- and Glycerol-Bound Galectin-3C by Neutron Crystallography to Guide Drug Design
- 2018
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Ingår i: Journal of Medicinal Chemistry. - : American Chemical Society (ACS). - 1520-4804 .- 0022-2623. ; 61:10, s. 4412-4420
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Tidskriftsartikel (refereegranskat)abstract
- The medically important drug target galectin-3 binds galactose-containing moieties on glycoproteins through an intricate pattern of hydrogen bonds to a largely polar surface-exposed binding site. All successful inhibitors of galectin-3 to date have been based on mono- or disaccharide cores closely resembling natural ligands. A detailed understanding of the H-bonding networks in these natural ligands will provide an improved foundation for the design of novel inhibitors. Neutron crystallography is an ideal technique to reveal the geometry of hydrogen bonds because the positions of hydrogen atoms are directly detected rather than being inferred from the positions of heavier atoms as in X-ray crystallography. We present three neutron crystal structures of the C-terminal carbohydrate recognition domain of galectin-3: the ligand-free form and the complexes with the natural substrate lactose and with glycerol, which mimics important interactions made by lactose. The neutron crystal structures reveal unambiguously the exquisite fine-tuning of the hydrogen bonding pattern in the binding site to the natural disaccharide ligand. The ligand-free structure shows that most of these hydrogen bonds are preserved even when the polar groups of the ligand are replaced by water molecules. The protonation states of all histidine residues in the protein are also revealed and correlate well with NMR observations. The structures give a solid starting point for molecular dynamics simulations and computational estimates of ligand binding affinity that will inform future drug design.
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- Manzoni, Francesco, et al.
(författare)
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Perdeuteration, crystallization, data collection and comparison of five neutron diffraction data sets of complexes of human galectin-3C
- 2016
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Ingår i: Acta Crystallographica Section D: Structural Biology. - 2059-7983. ; 72:11, s. 1194-1202
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Tidskriftsartikel (refereegranskat)abstract
- Galectin-3 is an important protein in molecular signalling events involving carbohydrate recognition, and an understanding of the hydrogen-bonding patterns in the carbohydrate-binding site of its C-terminal domain (galectin-3C) is important for the development of new potent inhibitors. The authors are studying these patterns using neutron crystallography. Here, the production of perdeuterated human galectin-3C and successive improvement in crystal size by the development of a crystal-growth protocol involving feeding of the crystallization drops are described. The larger crystals resulted in improved data quality and reduced data-collection times. Furthermore, protocols for complete removal of the lactose that is necessary for the production of large crystals of apo galectin-3C suitable for neutron diffraction are described. Five data sets have been collected at three different neutron sources from galectin-3C crystals of various volumes. It was possible to merge two of these to generate an almost complete neutron data set for the galectin-3C-lactose complex. These data sets provide insights into the crystal volumes and data-collection times necessary for the same system at sources with different technologies and data-collection strategies, and these insights are applicable to other systems.Perdeuteration, purification and the growth of large crystals of the carbohydrate-recognition domain of galectin-3C are described. Five neutron diffraction data sets have been collected at four neutron sources; these are compared and two are merged.
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