Is time the real line?

This paper is devoted to discussing the topological structure of the arrow of time. In the literature, it is often accepted that its algebraic and topological structures are that of a one-dimensional Euclidean space $\mathbb{E}^1$, although a critical review on the subject is not easy to be found. Hence, leveraging on an operational approach, we collect evidences to identify it structurally as a normed vector space $(\mathbb{Q}, |\cdot|)$, and take a leap of abstraction to complete it, up to isometries, to the real line. During the development of the paper, the space-time is recognized as a fibration, with the fibers being the sets of simultaneous events. The corresponding topology is also exposed: open sets naturally arise within our construction, showing that the classical space-time is non-Hausdorff. The transition from relativistic to classical regimes is explored too.Comment: 26 pages, 9 figures. Misprints corrected and minor adjustments according to the review proces

Generalization of the Extended Lagrangian Formalism on a Field Theory and Applications

Formalism of extended Lagrangian represent a systematic procedure to look for the local symmetries of a given Lagrangian action. In this work, the formalism is discussed and applied to a field theory. We describe it in detail for a field theory with first-class constraints present in the Hamiltonian formulation. The method is illustrated on examples of electrodynamics, Yang-Mills field and non-linear sigma model.Comment: 17 pages, to be published in Phys. Rev.

. Microwave-assisted solvothermal controlled synthesis of Fe-Co

Syntheses of bimetallic cobalt-iron-based nanoparticles starting from Co(acac)2 and Fe(acac)3 (acac = acetylacetonate) were carried out by microwave-assisted solvothermal process, using ethylene glycol as the solvent and (polyvinylpyrrolidone) PVP, as the stabilizer. Indeed, the reaction mechanism in the presence of ethylene glycol is well understood [1] with the role of PVP being the inhibition of nanoparticles growth [2]. However, the control of the morphology of the synthetized nanoparticles is still a great challenge. Herein, we demonstrated that by adding amines to the reaction mixture, it is possible to control the morphology of the prepared bimetallic cobalt-iron materials. Thus, different Co-Fe micro-composites were synthetized by an innovative microwave assisted solvothermal synthesis, which allows to considerably reduce reaction time from 12 h to 15 min, with respect to classical thermal methods. The procedure was optimized by varying several parameters, such as: amount of PVP, in the presence or in the absence of amines, reaction temperature. The dark brown obtained powders were characterized by scanning electron microscopy, infrared spectroscopy and thermogravimetric analysis, confirming the beneficial effect of the presence of the amine in the morphology of the obtained composites. The obtained results open a new scenario for further studies on the possibility to control the morphology of bimetallic composite materials. [1] Fievet F, Lagier J P and Figlarz M Mater. Res. Soc. Bull. 24 (1989) 29–34 [2] Teranishi T, Kurita R and Miyake M J. Inorg. Organometall. Polym. 10 (2000) 145–5

Resin-immobilized palladium nanoparticle catalysts for organic reactions in aqueous media: Morphological aspects

An insight into the nano- and micro-structural morphology of a polymer supported Pd catalyst employed in different catalytic reactions under green conditions is reported. The pre-catalyst was obtained by copolymerization of the metal-containing monomer Pd(AAEMA)2 [AAEMA = deprotonated form of 2-(acetoacetoxy) ethyl methacrylate] with ethyl methacrylate as co-monomer, and ethylene glycol dimethacrylate as cross-linker. This material was used in water for the Suzuki-Miyaura cross-coupling of aryl bromides, and for the reduction of nitroarenes and quinolines using NaBH4 or H2, as reductants. TEM analyses showed that in all cases the pristine Pd(II) species were reduced in situ to Pd(0), which formed metal nanoparticles (NPs, the real active species). The dependence of their average size (2-10 nm) and morphology on different parameters (temperature, reducing agent, presence of a phase transfer agent) is discussed. TEM and micro-IR analyses showed that the polymeric support retained its porosity and stability for several catalytic cycles in all reactions and Pd NPs did not aggregate after reuse. The metal nanoparticle distribution throughout the polymer matrix after several recycles provided precious information about the catalytic mechanism, which was truly heterogeneous in the hydrogenation reactions and of the so-called "release and catch" type in the Suzuki coupling

The cyanobacterial ribosomal-associated protein LrtA from Synechocystis sp. PCC 6803 is an oligomeric protein in solution with chameleonic sequence properties

The LrtA protein of Synechocystis sp. PCC 6803 intervenes in cyanobacterial post-stress survival and in stabilizing 70S ribosomal particles. It belongs to the hibernating promoting factor (HPF) family of proteins, involved in protein synthesis. In this work, we studied the conformational preferences and stability of isolated LrtA in solution. At physiological conditions, as shown by hydrodynamic techniques, LrtA was involved in a self-association equilibrium. As indicated by Nuclear Magnetic Resonance (NMR), circular dichroism (CD) and fluorescence, the protein acquired a folded, native-like conformation between pH 6.0 and 9.0. However, that conformation was not very stable, as suggested by thermal and chemical denaturations followed by CD and fluorescence. Theoretical studies of its highly-charged sequence suggest that LrtA had a Janus sequence, with a context-dependent fold. Our modelling and molecular dynamics (MD) simulations indicate that the protein adopted the same fold observed in other members of the HPF family ( - - - - - ) at its N-terminal region (residues 1–100), whereas the C terminus (residues 100–197) appeared disordered and collapsed, supporting the overall percentage of overall secondary structure obtained by CD deconvolution. Then, LrtA has a chameleonic sequence and it is the first member of the HPF family involved in a self-association equilibrium, when isolated in solution.Ministerio de Economía y Competitividad CTQ2015-64445-RMinisterio de Economía y Competitividad BIO2016-78020-RMinisterio de Economía y Competitividad FIS2014-52212-RMinisterio de Economía y Competitividad BIO2016-75634-PFundación Séneca 19353/PI/1

Residual helicity at the active site of the histidine phosphocarrier, HPr, modulates binding affinity to its natural partners

The phosphoenolpyruvate-dependent phosphotransferase system (PTS) modulates the preferential use of sugars in bacteria. The first proteins in the cascade are common to all organisms (EI and HPr). The active site of HPr involves a histidine (His15) located immediately before the beginning of the first a-helix. The regulator of sigma D (Rsd) protein also binds to HPr. The region of HPr comprising residues Gly9-Ala30 (HPr9–30), involving the first a-helix (Ala16-Thr27) and the preceding active site loop, binds to both the N-terminal region of EI and intact Rsd. HPr9–30 is mainly disordered. We attempted to improve the affinity of HPr9–30 to both proteins by mutating its sequence to increase its helicity. We designed peptides that led to a marginally larger population in solution of the helical structure of HPr9–30. Molecular simulations also suggested a modest increment in the helical population of mutants, when compared to the wild-type. The mutants, however, were bound with a less favorable affinity than the wild-type to both the N-terminal of EI (EIN) or Rsd, as tested by isothermal titration calorimetry and fluorescence. Furthermore, mutants showed lower antibacterial properties against Staphylococcus aureus than the wild-type peptide. The refore, we concluded that in HPr, a compromise between binding to its partners and residual structure at the active site must exist to carry out its function. © 2021 by the authors. Licensee MDPI, Basel, Switzerland

Dynamics of the Intrinsically Disordered Inhibitor IF7 of Glutamine Synthetase in Isolation and in Complex with its Partner

Glutamine synthetase (GS) catalyzes the ATP-dependent formation of glutamine from glutamate and ammonia. The activity of Synechocystis sp. PCC 6803 GS is regulated, among other mechanisms, by protein-protein interactions with a 65-residue-long, intrinsically disordered protein (IDP), named IF7. IDPs explore diverse conformations in their free states and, in some cases, in their molecular complexes. We used both nuclear magnetic resonance (NMR) at 11.7 T and small angle X-ray scattering (SAXS) to study the size and the dynamics in the picoseconds-to-nanosecond (ps-ns) timescale of: (i) isolated IF7; and (ii) the IF7/GS complex. Our SAXS findings, together with MD results, show: (i) some of the possible IF7 structures in solution; and, (ii) that the presence of IF7 affected the structure of GS in solution. The joint use of SAXS and NMR shows that movements of each amino acid of IF7 were uncorrelated with those of its neighbors. Residues of IF7 with the largest values of the relaxation rates (R1, R2 and ηxy), in the free and bound species, were mainly clustered around: (i) the C terminus of the protein; and (ii) Ala30. These residues, together with Arg8 (which is a hot-spot residue in the interaction with GS), had a restricted mobility in the presence of GS. The C-terminal region, which appeared more compact in our MD simulations of isolated IF7, seemed to be involved in non-native contacts with GS that help in the binding between the two macromolecules.Ministerio de Economía y Competitividad RTI 2018-097991- BI0