Search results for "Hydration water"

showing 7 items of 7 documents

Lead(II) ions adsorption onto amyloid particulates: An in depth study

2022

The production of new cost-effective biocompatible sorbent sustainable materials, with natural origins, able to remove heavy metals from water resources is nowadays highly desirable in order to reduce pollution and increase clean water availability. In this context, self-assembled protein materials with amyloid structures seem to have a great potential as natural platform for a broader development of highly-tunable structures. In this work we show how protein particulates, a generic form of protein aggregates, with spherical micro sized shape can be used as adsorbents of Pb2+ ions from aqueous solution. The effect of pH, ionic medium, ionic strength and temperature of the metal ion solution…

IonsMetal pollutionTemperatureRemediationWaterHydrogen-Ion ConcentrationEnvironmental pollutionHydration waterSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Surfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsWater PurificationBiomaterialsKineticsColloid and Surface ChemistryBovine serum albuminLeadMetals HeavySettore CHIM/01 - Chimica AnaliticaAdsorptionAmyloid superstructuresWater Pollutants Chemical
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3D MICROSIZED PROTEIN AMYLOID PARTICULATES AS EFFECTIVE BIOADSORBERS FOR Pb2+ IONS

The production of new cost-effective biocompatible sorbent sustainable materials, with natural origins, able to remove heavy metals from water resources is nowadays highly desirable in order to reduce pollution and increase clean water availability. In this context, self-assembled protein materials with highly ordered amyloid structures, stabilised by H-bonds, seems to have a great potential as natural platform for a broader development of highly-tunable structures. By suitably varying solution conditions it is possible to tune aggregate size, surface area and morphologies as well as their physicochemical (hydrophobicity, hydrophilicity, swelling/deswelling properties) and mechanical proper…

lead bovine serum albumin amyloid superstructures adsorption remediation hydration water metal pollution environmental pollution
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Decoding vibrational states of Concanavalin A amyloid fibrils.

2015

International audience; Amyloid and amyloid-like fibrils are a general class of protein aggregates and represent a central topic in life sciences for their involvement in several neurodegenerative disorders and their unique mechanical and supramolecular morphological properties. Both their biological role and their physical properties, including their high mechanical stability and thermodynamic inertia, are related to the structural arrangement of proteins in the aggregates at molecular level. Significant variations may exist in the supramolecular organization of the commonly termed cross-β structure that constitutes the amyloid core. In this context, a fine knowledge of the structural deta…

AmyloidAbsorption spectroscopy[SDV]Life Sciences [q-bio]BiophysicsSupramolecular chemistry02 engineering and technologymacromolecular substancesProtein aggregationAntiparallel (biochemistry)FibrilSpectrum Analysis RamanBiochemistryVibrationProtein Structure Secondary03 medical and health sciencessymbols.namesakeSpectroscopy Fourier Transform InfraredConcanavalin AHumansFourier transform infrared spectroscopyRaman030304 developmental biology0303 health sciencesChemistryOrganic ChemistryIntermolecular force021001 nanoscience & nanotechnologyAmyloid FTIR RAMAN hydration water THz spectroscopy[SDV] Life Sciences [q-bio]CrystallographyFTIRTerahertz spectroscopysymbolsBiophysicsFibrils0210 nano-technologyRaman spectroscopy
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Anharmonic activations in proteins and peptide model systems and their connection with supercooled water thermodynamics

2016

International audience; — Proteins, the nano-machines of living systems, are highly dynamic molecules. The timescale of functionally relevant motions spans over a very broad range, from femtoseconds to several seconds. In particular, the pico-to nanoseconds region is characterized by side-chain and backbone anharmonic fluctuations that are responsible for many biological tasks like ligand binding, substrate recognition and enzymatic activity. Neutron scattering on hydrated protein powders reveals two main activations of anharmonic dynamics, characterized by different onset temperature and amplitude. Here we review our work on synthetic polypeptides, native proteins, and single amino acids t…

Quantitative Biology::Biomolecules[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM][SDV]Life Sciences [q-bio][SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyNeutron scatteringProtein dynamicsLiquid-liquid crossoverComputingMilieux_MISCELLANEOUSHydration waterSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)
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THE PHYSICAL ORIGIN OF PROTEIN DYNAMICAL TRANSITION: A LIQUID-LIQUID TRANSITION IN HYDRATION WATER?

2015

In this thesis I study, by means of neutron scattering, calorimetry, and dielectric spectroscopy, the physical origin of protein dynamical transition (PDT) which is usually observed at ~230 K in protein hydrated powders and is deemed necessary for protein function. Measurements reported in this thesis have been performed on hydrated powders of Myoglobin. The combined use of different experimental techniques gives a coherent description of the PDT and reveals a connection with a liquid-liquid crossover occurring in the protein hydration water at about the same temperature. In order to deepen our understanding of this connection and to obtain a direct experimental evidence of the existence of…

deeply cooled confined waterprotein/hydration water relaxationphysical origin of the protein dynamical transitionprotein dynamical transitionhydration water liquid–liquid transitionProtein dynamicglass transitionequilibrium fluctuationdisordered silica xerogelSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)
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The geochemical riddle of “low-salinity gypsum” deposits

2022

International audience; Gypsum makes up about one fifth of giant salt deposits formed by evaporation of seawater throughout Earth’s history. Although thermodynamic calculations and precipitation experiments predict that gypsum precipitates when the salinity of evaporating seawater attains about 110 g kg-1, gypsum deposits of the Mediterranean Salt Giant often bear the geochemical signature of precipitation from less saline water masses. Addressing this geochemical riddle is important because marine gypsum deposition and continental gypsum erosion affect the global carbon cycle. We investigated gypsum deposits formed in the marginal basins of the Mediterranean Sea during the Messinian Salini…

Geochemistry and Petrology[SDU.STU.GC]Sciences of the Universe [physics]/Earth Sciences/GeochemistryGeochemical modelingLow-salinity gypsumSettore GEO/01 - Paleontologia E PaleoecologiaHydration water isotopes (δBiogeochemical S cycleFluid inclusionsSettore GEO/08 - Geochimica E Vulcanologia
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Hydration dependence of myoglobin dynamics studied with elastic neutron scattering, differential scanning calorimetry and broadband dielectric spectr…

2014

In this work we present a thorough investigation of the hydration dependence of myoglobin dynamics. The study is performed on D2O-hydrated protein powders in the hydration range 0<h<0.5 (h≡gr[D2O]/gr[protein]) and in the temperature range 20-300K. The protein equilibrium fluctuations are investigated with Elastic Neutron Scattering using the spectrometer IN13 at ILL (Grenoble), while the relaxations of the protein + hydration water system are investigated with Broadband Dielectric Spectroscopy; finally, Differential Scanning Calorimetry is used to obtain a thermodynamic description of the system. The effect of increasing hydration is to speed up the relaxations of the myoglobin + hydration …

inorganic chemicalsWork (thermodynamics)BiophysicsNeutron scatteringMolecular Dynamics SimulationBiochemistryPhase Transitionchemistry.chemical_compoundDifferential scanning calorimetryAnimalsHorsesRange (particle radiation)Calorimetry Differential ScanningMyoglobinProtein dynamicsOrganic ChemistryDynamics (mechanics)WaterSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Neutron DiffractionMyoglobinchemistryChemical physicsDielectric SpectroscopyPhysical chemistryGlass transition•Protein dynamics •Equilibrium fluctuations •Protein/hydration water relaxations •Glass transition •Hydration water liquid-liquid transitionBiophysical chemistry
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