Browsing by Author "Nelson, ARJ"

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    Advice on describing Bayesian analysis of neutron and X-ray reflectometry
    (International Union of Crystallography (IUCr), 2023) McCluskey, AR; Caruana, AJ; Kinane, CJ; Armstrong, AJ; Arnold, T; Cooper, JFK; Cortie, DL; Hughes, AV; Moulin, JF; Nelson, ARJ; Potrezbowski, W; Starostin, V
    As a result of the availability of modern software and hardware, Bayesian analysis is becoming more popular in neutron and X-ray reflectometry analysis. The understandability and replicability of these analyses may be harmed by inconsistencies in how the probability distributions central to Bayesian methods are represented in the literature. Herein advice is provided on how to report the results of Bayesian analysis as applied to neutron and X-ray reflectometry. This includes the clear reporting of initial starting conditions, the prior probabilities, the results of any analysis and the posterior probabilities that are the Bayesian equivalent of the error bar, to enable replicability and improve understanding. It is believed that this advice, grounded in the authors' experience working in the field, will enable greater analytical reproducibility in the work of the reflectometry community, and improve the quality and usability of results. © 2023 The Authors. Open Access published under a CC BY 4.0 licence.
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    Advice on describing Bayesian analysis of neutron and x-ray reflectometry
    (International Union of Crystallography, 2023-02-01) McCluskey, AR; Caruana, AJ; Kinane, CJ; Armstrong, AJ; Arnold, T; Cooper, JFK; Cortie, DL; Hughes, AV; Moulin, JF; Nelson, ARJ; Potrzebowski, W; Starostin, V
    As a result of the availability of modern software and hardware, Bayesian analysis is becoming more popular in neutron and X-ray reflectometry analysis. The understandability and replicability of these analyses may be harmed by inconsistencies in how the probability distributions central to Bayesian methods are represented in the literature. Herein advice is provided on how to report the results of Bayesian analysis as applied to neutron and X-ray reflectometry. This includes the clear reporting of initial starting conditions, the prior probabilities, the results of any analysis and the posterior probabilities that are the Bayesian equivalent of the error bar, to enable replicability and improve understanding. It is believed that this advice, grounded in the authors' experience working in the field, will enable greater analytical reproducibility in the work of the reflectometry community, and improve the quality and usability of results. © The Authors CC BY 4.0
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    The assembly mechanism and mesoscale architecture of protein–polysaccharide complexes formed at the solid–liquid Interface
    (American Chemical Society, 2022-10-04) Biswas, S; Melton, LD; Nelson, ARJ; Le Brun, AP; Heinrich, F; McGillivray, DJ; Xu, AY
    Protein-polysaccharide composite materials have generated much interest due to their potential use in medical science and biotechnology. A comprehensive understanding of the assembly mechanism and the mesoscale architecture is needed for fabricating protein-polysaccharide composite materials with desired properties. In this study, complex assemblies were built on silica surfaces through a layer-by-layer (LbL) approach using bovine beta-lactoglobulin variant A (βLgA) and pectin as model protein and polysaccharide, respectively. We demonstrated the combined use of quartz crystal microbalance with dissipation monitoring (QCM-D) and neutron reflectometry (NR) for elucidating the assembly mechanism as well as the internal architecture of the protein-polysaccharide complexes formed at the solid-liquid interface. Our results show that βLgA and pectin interacted with each other and formed a cohesive matrix structure at the interface consisting of intertwined pectin chains that were cross-linked by βLgA-rich domains. Although the complexes were fabricated in an LbL fashion, the complexes appeared to be relatively homogeneous with βLgA and pectin molecules spatially distributed within the matrix structure. Our results also demonstrate that the density of βLgA-pectin complex assemblies increased with both the overall and local charge density of pectin molecules. Therefore, the physical properties of the protein-polysaccharide matrix structure, including density and level of hydration, can be tuned by using polysaccharides with varying charge patterns, thus promoting the development of composite materials with desired properties. © 2024 American Chemical Society