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661 items found (0 items not approved), displaying 1 to 10.[First/Prev] 1, 2, 3, 4, 5, 6, 7, 8 [Next/Last]

Instruments / Technical Area	Publication Details	Published
I22-Small angle scattering & Diffraction	Tailoring viscoelastic properties of dynamic supramolecular poly(butadiene)-based elastomers M. Hyder , A. D. O'Donnell , A. M. Chippindale , I.m. German , J.l. Harries , O. Shebanova , I. W. Hamley , W. Hayes Materials Today Chemistry 26 DOI: 10.1016/j.mtchem.2022.101008 Diamond Proposal Number(s): [22909] Open Access Show Abstract ▼ Abstract: The discovery and development of new adhesive materials is critical for real-world applications of polymeric composite materials. Herein, we report the design and synthesis of a library of structurally related phase-separated supramolecular polyurethanes whose mechanical properties and adhesive characteristics can be enhanced through minor structural modifications of the polymer end-group. The interplay between phase separation of the hard domain polar end-groups and soft polybutadiene domains, coupled with tuneable self-assembly afforded by the polar end-groups, gives rise to a class of materials with tuneable mechanical properties. Exceptionally strong supramolecular adhesives and mechanically robust self-healing elastomers were identified. The mechanical properties were investigated through tensile testing. Finally, rheological analysis of the supramolecular materials was used to identify suitable healing and adhesive temperatures in addition to elucidate the supramolecular polyurethanes' thermal-responsive nature.	Dec 2022
B21-High Throughput SAXS	Flavour compounds affect protein structure: The effect of methyl anthranilate on bovine serum albumin conformation Vlad Dinu , Pallab Kumar Borah , Molly Muleya , David J Scott , Ryan Lithgo , Jacob Pattem , Stephen E. Harding , Gleb E. Yakubov , Ian D. Fisk Food Chemistry 388 DOI: 10.1016/j.foodchem.2022.133013 Diamond Proposal Number(s): [22113] Show Abstract ▼ Abstract: This study aims to understand possible effects of flavour compounds on the structure and conformation of endogenous proteins. Using methyl anthranilate (a grape flavour compound added to drinks, confectionery, and vape-liquids) and bovine serum albumin (BSA, a model serum protein) we designed experimental investigations using analytical ultracentrifugation, size exclusion chromatography small angle X-ray scattering, and fluorescence spectroscopy to reveal that methyl anthranilate spontaneously binds to BSA (ΔG°, ca. −21 KJ mol−1) which induces a conformational compactness (ca. 10 %) in the monomer structure. Complementary molecular modelling and dynamics simulations suggested the binding occurs at Sudlow II of BSA via establishment of hydrogen bonds with arginine409, lysine413 and serine488 leading to an increased conformational order in domains IA, IIB and IIIB. This work aims to set the foundation for future research on flavour-protein interactions and offer new sets of opportunities for understanding the effects of small compounds on protein structure.	Sep 2022
I22-Small angle scattering & Diffraction	A structural study of the self-association of different starches in presence of bacterial cellulose fibrils P. Díaz-Calderón , E. Simone , A. I. I. Tyler , J. Enrione , T. Foster Carbohydrate Polymers 288 DOI: 10.1016/j.carbpol.2022.119361 Diamond Proposal Number(s): [22659] Show Abstract ▼ Abstract: A multi-analytical study was performed to analyse the effect of bacterial cellulose (BCF) on the self-association of starches with different amylose content (wheat, waxy-maize), assessing macrostructural properties (rheology, gel strength) and some nano and sub-nano level features (small and wide-angle X-ray scattering). Although pasting viscosities and G′ were significantly increased by BCF in both starches, cellulose did not seem to promote the self-association of amylose in short-range retrogradation. A less elastic structure was reflected by a 2–3-fold increase in loss factor (G″/G′) at the highest BCF concentration tested. This behavior agreed with the nano and sub-nano characterisation of the samples, which showed loss of starch lamellarity and incomplete full recovery of an ordered structure after storage at 4 °C for 24 h. The gel strength data could be explained by the contribution of BCF to the mechanical response of the sample. The information gained in this work is relevant for tuning the structure of tailored starch-cellulose composites.	Jul 2022
B21-High Throughput SAXS	Exploring Calbindin-IMPase fusion proteins structure and activity James Noble , John R. Atack Biochemistry And Biophysics Reports 30 DOI: 10.1016/j.bbrep.2022.101266 Diamond Proposal Number(s): [14891] Open Access Show Abstract ▼ Abstract: Calbindin-D28k is a calcium binding protein that is highly expressed in the mammalian central nervous system. It has been reported that calbindin-D28k binds to and increases the activity of inositol Monophosphatase (IMPase). This is an enzyme that is involved in the homeostasis of the Inositol trisphosphate signalling cascade by catalysing the final dephosphorylation of inositol and has been implicated in the therapeutic mechanism of lithium treatment of bipolar disorder. Previously studies have shown that calbindin-D28k can increase IMPase activity by up to 250 hundred-fold. A preliminary in silico model was proposed for the interaction. Here, we aimed at exploring the shape and properties of the calbindin-IMPase complex to gain new insights on this biologically important interaction. We created several fusion constructs of calbindin-D28k and IMPase, connected by flexible amino acid linkers of different lengths and orientations to fuse the termini of the two proteins together. The resulting fusion proteins have activities 200%–400% higher the isolated wild-type IMPase. The constructs were characterized by small angle X-ray scattering to gain information on the overall shape of the complexes and validate the previous model. The fusion proteins form a V-shaped, elongated and less compact complex as compared to the model. Our results shed new light into this protein-protein interaction.	Jul 2022
B21-High Throughput SAXS	3D-printed SAXS chamber for controlled in situ dialysis and optical characterization Tamara Ehm , Julian Philipp , Martin Barkey , Martina Ober , Achim Theo Brinkop , David Simml , Miriam Von Westphalen , Bert Nickel , Roy Beck , Joachim O. Rädler Journal Of Synchrotron Radiation 29 DOI: 10.1107/S1600577522005136 Diamond Proposal Number(s): [24693, 21971] Open Access Show Abstract ▼ Abstract: 3D printing changes the scope of how samples can be mounted for small-angle X-ray scattering (SAXS). In this paper a 3D-printed X-ray chamber, which allows for in situ exchange of buffer and in situ optical transmission spectroscopy, is presented. The chamber is made of cyclic olefin copolymers (COC), including COC X-ray windows providing ultra-low SAXS background. The design integrates a membrane insert for in situ dialysis of the 100 µl sample volume against a reservoir, which enables measurements of the same sample under multiple conditions using an in-house X-ray setup equipped with a 17.4 keV molybdenum source. The design's capabilities are demonstrated by measuring reversible structural changes in lipid and polymer systems as a function of salt concentration and pH. In the same chambers optical light transmission spectroscopy was carried out measuring the optical turbidity of the mesophases and local pH values using pH-responsive dyes. Microfluidic exchange and optical spectroscopy combined with in situ X-ray scattering enables vast applications for the study of responsive materials.	Jul 2022
B21-High Throughput SAXS	Non-ionic detergent assists formation of supercharged nanodiscs and insertion of membrane proteins Frederik G. Tidemand , Sara Blemmer , Nicolai T. Johansen , Lise Arleth , Martin Cramer Pedersen Biochimica Et Biophysica Acta (bba) - Biomembranes 1864 DOI: 10.1016/j.bbamem.2022.183884 Diamond Proposal Number(s): [23041, 27887] Open Access Show Abstract ▼ Abstract: Nanodiscs are used to stabilize membrane proteins in a lipid environment and enable investigations of the function and structure of these. Membrane proteins are often only available in small amounts, and thus the stability and ease of use of the nanodiscs are essential. We have recently explored circularizing and supercharging membrane scaffolding proteins (MSPs) for nanodisc formation and found increased temporal stability at elevated temperatures. In the present study, we investigate six different supercharged MSPs and their ability to form nanodiscs: three covalently circularized and the three non-circularized, linear versions. Using standard reconstitution protocols using cholate as the reconstitution detergent, we found that two of the linear constructs formed multiple lipid-protein species, whereas adding n-Dodecyl-B-D-maltoside (DDM) with the cholate in the reconstitution gave rise to single-species nanodisc formation for these MSPs. For all MSPs, the formed nanodiscs were analyzed by small-angle X-ray scattering (SAXS), which showed similar structures for each MSP, respectively, suggesting that the structures of the formed nanodiscs are independent of the initial DDM content, as long as cholate is present. Lastly, we incorporated the membrane protein proteorhodopsin into the supercharged nanodiscs and observed a considerable increase in incorporation yield with the addition of DDM. For the three circularized MSPs, a single major species appeared in the size exclusion chromatography (SEC) chromatogram, suggesting monodisperse nanodiscs with proteorhodopsin incorporated, which is in strong contrast to the samples without DDM showing almost no incorporation and high polydispersity.	Jun 2022
I22-Small angle scattering & Diffraction	The hierarchical response of human corneal collagen to controlled inflation James Bell , Sian R. Morgan , Elena Koudouna , Sally Hayes , Keith M. Meek 2022 ARVO Annual Meeting Show Abstract ▼ Abstract: Purpose : To elucidate the hierarchical deformation mechanisms of human corneal collagen under controlled inflation of physiological and pathological magnitudes. Methods : 6 human donor corneas with scleral rim were mounted onto a bespoke sealed cell, which was connected via two pressure regulators and an expansion vessel to a source of compressed nitrogen. The cell included a window transparent to X-rays and was connected to translation and rotation stages inside beamline I22 at the Diamond Light Source synchrotron, UK. Images were acquired naso-temporally across the cornea from limbus to limbus at intraocular pressures of 5.5 mmHg, 17.5 mmHg and 40 mmHg. These increments were chosen for comparison with previous static results in the literature and to mimic the normal physiological state and ocular hypertension. Results : The inflation apparatus was able to maintain pressure to an accuracy better than 0.1 mmHg. Features corresponding to collagen fibril diameter, spacing, D-period and orientation as well as tropocollagen spacing and orientation were measured simultaneously. Preliminary analysis revealed a radial distribution of strain (manifested as a change in D-period) across the cornea, which was accentuated in the outer periphery and limbus. In general, the interfibrillar spacing in the periphery and limbus (where collagen fibrils are arranged circumferentially) was found to increase with pressure. Conclusions : The trends in D-period strain are indicative of bulging under increased pressure, which is pronounced at the limbus and the outer periphery. This agrees with the general consensus that the outer periphery and limbus act as a buffer zone, which takes up most of the strain under changes in intraocular pressure, and thus minimises changes in focussing power of the cornea. Further in-depth analysis of this data will allow us to calculate the supramolecular twist (which gives rise to a spring-like stretch in collagen fibrils) and examine in more detail the hierarchical response of corneal collagen to changes in intraocular pressures.	Jun 2022
B21-High Throughput SAXS I03-Macromolecular Crystallography I04-Macromolecular Crystallography	Primary and secondary functions of HLA-E are determined by stability and conformation of the peptide-bound complexes Lucy C. Walters , Daniel Rozbesky , Karl Harlos , Max Quastel , Hong Sun , Sebastian Springer , Robert P. Rambo , Fiyaz Mohammed , E. Yvonne Jones , Andrew J. Mcmichael , Geraldine M. Gillespie Cell Reports 39 DOI: 10.1016/j.celrep.2022.110959 Diamond Proposal Number(s): [19946] Open Access Show Abstract ▼ Abstract: MHC-E regulates NK cells by displaying MHC class Ia signal peptides (VL9) to NKG2A:CD94 receptors. MHC-E can also present sequence-diverse, lower-affinity, pathogen-derived peptides to T cell receptors (TCRs) on CD8+ T cells. To understand these affinity differences, human MHC-E (HLA-E)-VL9 versus pathogen-derived peptide structures are compared. Small-angle X-ray scatter (SAXS) measures biophysical parameters in solution, allowing comparison with crystal structures. For HLA-E-VL9, there is concordance between SAXS and crystal parameters. In contrast, HLA-E-bound pathogen-derived peptides produce larger SAXS dimensions that reduce to their crystallographic dimensions only when excess peptide is supplied. Further crystallographic analysis demonstrates three amino acids, exclusive to MHC-E, that not only position VL9 close to the α2 helix, but also allow non-VL9 peptide binding with re-configuration of a key TCR-interacting α2 region. Thus, non-VL9-bound peptides introduce an alternative peptide-binding motif and surface recognition landscape, providing a likely basis for VL9- and non-VL9-HLA-E immune discrimination.	Jun 2022
B21-High Throughput SAXS	Minimalistic ice recrystallisation inhibitors based on phenylalanine Matthew T. Warren , Iain Galpin , Muhammad Hasan , Steve Hindmarsh , John Padrnos , Charlotte J. C. Edwards-Gayle , Robert T. Mathers , Dave J. Adams , Gabriele Cesare Sosso , Matthew Ian Gibson Chemical Communications DOI: 10.1039/D2CC02531K Diamond Proposal Number(s): [29985] Open Access Show Abstract ▼ Abstract: Ice recrystallisation inhibition (IRI) is typically associated with ice binding proteins, but polymers and other mimetics are emerging. Here we identify phenylalanine as a minimalistic, yet potent, small-molecule IRI capable of inhibiting ice growth at just 1 mg.mL-1. Facial amphiphilicity is shown to be a crucial structural feature, with para-substituents enhancing (hydrophobic) or decreasing (hydrophilic) activity. Both amino and acid groups were found to be essential. Solution-phase self-assembly of Phenylalanine was not observed, but the role of self-assembly at the ice/water interface could not be ruled out as a contributing factor.	Jun 2022
B21-High Throughput SAXS	Biophysical characterisation of human LincRNA-p21 sense and antisense Alu inverted repeats Michael H D'Souza , Tyler Mrozowich , Maulik D. Badmalia , Mitchell Geeraert , Angela Frederickson , Amy Henrickson , Borries Demeler , Michael t. Wolfinger , Trushar R. Patel Nucleic Acids Research 50, 5881 - 5898 DOI: 10.1093/nar/gkac414 Diamond Proposal Number(s): [26855] Open Access Show Abstract ▼ Abstract: Human Long Intergenic Noncoding RNA-p21 (LincRNA-p21) is a regulatory noncoding RNA that plays an important role in promoting apoptosis. LincRNA-p21 is also critical in down-regulating many p53 target genes through its interaction with a p53 repressive complex. The interaction between LincRNA-p21 and the repressive complex is likely dependent on the RNA tertiary structure. Previous studies have determined the two-dimensional secondary structures of the sense and antisense human LincRNA-p21 AluSx1 IRs using SHAPE. However, there were no insights into its three-dimensional structure. Therefore, we in vitro transcribed the sense and antisense regions of LincRNA-p21 AluSx1 Inverted Repeats (IRs) and performed analytical ultracentrifugation, size exclusion chromatography, light scattering, and small angle X-ray scattering (SAXS) studies. Based on these studies, we determined low-resolution, three-dimensional structures of sense and antisense LincRNA-p21. By adapting previously known two-dimensional information, we calculated their sense and antisense high-resolution models and determined that they agree with the low-resolution structures determined using SAXS. Thus, our integrated approach provides insights into the structure of LincRNA-p21 Alu IRs. Our study also offers a viable pipeline for combining the secondary structure information with biophysical and computational studies to obtain high-resolution atomistic models for long noncoding RNAs.	Jun 2022

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