Modelling human choices: MADeM and decision‑making

Research supported by FAPESP 2015/50122-0 and DFG-GRTK 1740/2. RP and AR are also part of the Research, Innovation and Dissemination Center for Neuromathematics FAPESP grant (2013/07699-0). RP is supported by a FAPESP scholarship (2013/25667-8). ACR is partially supported by a CNPq fellowship (grant 306251/2014-0)

Ferrite precipitation in quaternary Fe–C–X1–X2 systems using high-throughput approaches

This study investigates the effect of composition on ferrite growth kinetics in quaternary Fe–C–X1–X2 systems (X: Ni, Cr, Mo) using a high-throughput methodology. This study provides the largest dataset to date on ferrite growth kinetics in multi-component steels, offering novel insight into the behavior of these complex systems. To this end, high-energy X-ray diffraction is utilized to gather kinetic data in situ along composition gradients, leading to the measurement of phase transformation kinetics maps in compositional space. The obtained data is compared to predictions from various models describing ferrite growth kinetics in low-alloy steels. The modified "three-jump" solute drag model is shown to describe best the ferrite growth kinetics in these quaternary systems, without the need for additional calibration or fitting parameters. The success of this model is attributed to its consideration of individual solute interactions with the interface and inter-elemental interactions. The findings of this study provide valuable insight for robust modeling of phase transformations and microstructural evolution in multi-component steels, a critical tool in accelerating alloy optimization and in enhancing process control

Structural insights into a cooperative switch between one and two FimH bacterial adhesins binding pauci- and high-mannose type N-glycan receptors

The FimH type-1 fimbrial adhesin allows pathogenic Escherichia coli to adhere to glycoproteins in the epithelial linings of human bladder and intestinal tract, by using multiple fimbriae simultaneously. Pauci- and high-mannose type N-glycans are natural FimH receptors on those glycoproteins. Oligomannose-3 and oligomannose-5 bind with the highest affinity to FimH by using the same Manα1,3Man branch. Oligomannose-6 is generated from oligomannose-5 in the next step of the biogenesis of high-mannose N-glycans, by the transfer of a mannose in α1,2-linkage onto this branch. Using serial crystallography and by measuring the kinetics of binding, we demonstrate that shielding the high-affinity epitope drives the binding of multiple FimH molecules. First, we profiled FimH glycan binding on a microarray containing paucimannosidic N-glycans and in a FimH LEctPROFILE assay. To make the transition to oligomannose-6, we measured the kinetics of FimH binding using paucimannosidic N-glycans, glycoproteins and all four α-dimannosides conjugated to bovine serum albumin. Equimolar mixed interfaces of the dimannosides present in oligomannose-6 and molecular dynamics simulations suggest a positive cooperativity in the bivalent binding of Manα1,3Manα1 and Manα1,6Manα1 dimannosides. The binding of core α1,6-fucosylated oligomannose-3 in cocrystals of FimH is monovalent but interestingly the GlcNAc1—Fuc moiety retains highly flexibility. In cocrystals with oligomannose-6, two FimH bacterial adhesins bind the Manα1,3Manα1 and Manα1,6Manα1 endings of the second trimannose core (A-4′-B). This cooperative switch towards bivalent binding appears sustainable beyond a molar excess of oligomannose-6. Our findings provide important novel structural insights for the design of multivalent FimH antagonists that bind with positive cooperativity

Behavior of nearby synchronous rotations of a Poincaré–Hough satellite at low eccentricity

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