0000000000501311

AUTHOR

Francesca Natali

0000-0002-1631-4624

showing 15 related works from this author

The protein dynamical transition does not require the protein polypeptide chain

2011

We give experimental evidence that the main features of protein dynamics revealed by neutron scattering, i.e., the “protein dynamical transition” and the “boson peak”, do not need the protein polypeptide chain. We show that a rapid increase of hydrogen atoms fluctuations at about 220 K, analogous to the one observed in hydrated myoglobin powders, is also observed in a hydrated amino acids mixture with the chemical composition of myoglobin but lacking the polypeptide chain; in agreement with the protein behavior, the transition is abolished in the dry mixture. Further, an excess of low-frequency vibrational modes around 3 meV, typically observed in protein powders, is also observed in our mi…

chemistry.chemical_classificationHydrogenProtein dynamicsProtein mean square displacementchemistry.chemical_elementNeutron scatteringHydrated powdersInelastic neutron scatteringAmino acidAmino acidCrystallographychemistry.chemical_compoundchemistryMyoglobinMolecular vibrationSide chainProtein dynamicGeneral Materials ScienceElastic neutron scatteringPhysical and Theoretical ChemistryChemical composition
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Proton dynamics in bacterial spores, a neutron scattering investigation

2014

International audience; Results from first neutron scattering experiments on bacterial spores are reported. The elastic intensities and mean square displacements have a non-linear behaviour as function of temperature, which is in agreement with a model presenting more pronounced variations at around 330 K (57 • C) and 400 K (127 • C). Based on the available literature on thermal properties of bacterial spores, mainly referring to differential scanning calorimetry, they are suggested to be associated to main endothermic transitions induced by coat and/or core bacterial response to heat treatment.

Mean squareProton[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]ChemistryPhysicsQC1-999[PHYS.PHYS.PHYS-BIO-PH]Physics [physics]/Physics [physics]/Biological Physics [physics.bio-ph]Dynamics (mechanics)neutron scatteringAnalytical chemistryNeutron scattering[ SDV.MP.BAC ] Life Sciences [q-bio]/Microbiology and Parasitology/BacteriologyEndothermic processEndospore[SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/BacteriologyCrystallographybacterial sporesDifferential scanning calorimetry[ PHYS.PHYS.PHYS-BIO-PH ] Physics [physics]/Physics [physics]/Biological Physics [physics.bio-ph]Thermal[ SDV.BBM.BS ] Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM]
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Physical Origin of Anharmonic Dynamics in Proteins: New Insights From Resolution-Dependent Neutron Scattering on Homomeric Polypeptides

2012

Neutron scattering reveals a complex dynamics in polypeptide chains, with two main onsets of anharmonicity whose physical origin and biological role are still debated. In this study the dynamics of strategically selected homomeric polypeptides is investigated with elastic neutron scattering using different energy resolutions and compared with that of a real protein. Our data spotlight the dependence of anharmonic transition temperatures and fluctuation amplitudes on energy resolution, which we quantitatively explain in terms of a two-site model for the protein-hydration water energy landscape. Experimental data strongly suggest that the protein dynamical transition is not a mere resolution …

PhysicsQuantitative Biology::BiomoleculesfluctuationsResolution (electron density)AnharmonicityProtein dynamical transitionProteinsGeneral Physics and AstronomyNeutron scatteringMolecular physicsPhase TransitionSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Neutron DiffractionComplex dynamicsAmplitudeModels ChemicalBiophysicsHomomericProtein dynamicConnection (algebraic framework)PeptidesEnergy (signal processing)
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Hydration dependent dynamics in sol-gel encapsulated myoglobin.

2008

In this work we study the effect of hydration on the dynamics of a protein in confined geometry, i.e. encapsulated in a porous silica matrix. Using elastic neutron scattering we investigate the temperature dependence of the mean square displacements of non-exchangeable hydrogen atoms of sol-gel encapsulated met-myoglobin. The study is extended to samples at 0.2, 0.3 and 0.5 g water/g protein fractions and comparison is made with met-myoglobin powders at the same average hydration and with a dry powder sample. Elastic data are analysed using a model of dynamical heterogeneity to take into account deviations of elastic intensity from gaussian behaviour in a large momentum transfer range and r…

HydrogenBiophysicsHydrationchemistry.chemical_elementSol–gelNeutron scatteringELASTIC NEUTRON-SCATTERINGPROTEIN HYDRATIONAnimalsDynamical heterogeneityPorositySol-gelSPECTROSCOPYMyoglobinProtein dynamicsSolvent dynamicMomentum transferTemperatureWaterGeneral MedicineElasticityCrystallographyNeutron DiffractionSolvation shellchemistryChemical physicsProtein dynamicSilica hydrogelsGelsTRANSITIONHydrogenEuropean biophysics journal : EBJ
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Direct Evidence of the Amino Acid Side Chain and Backbone Contributions to Protein Anharmonicity

2010

Elastic incoherent neutron scattering has been used to study the temperature dependence of the mean-square displacements of nonexchangeable hydrogen atoms in powders of a series of homomeric polypeptides (polyglycine, polyalanine, polyphenylalanine and polyisoleucine) in comparison with myoglobin at the same hydration level (h = 0.2). The aim of the work was to measure the dynamic behavior of different amino acid residues separately and assess the contribution of each type of side chain to the anharmonic dynamics of proteins. The results provide direct experimental evidence that the first anharmonic activation, at approximately 150 K, is largely due to methyl group rotations entering the ti…

ChemistryStereochemistryDirect evidenceMyoglobinAnharmonicityProteinsGeneral ChemistryNeutron scatteringNeutron scatteringMolecular Dynamics SimulationRing (chemistry)BiochemistryCatalysisProtein Structure Secondarychemistry.chemical_compoundCrystallographyColloid and Surface ChemistryMyoglobinSide chainProtein dynamicMethyleneAmino AcidsPeptidesMethyl group
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Incoherent elastic and quasi-elastic neutron scattering investigation of hemoglobin dynamics.

2005

In this work we investigate the dynamic properties of hemoglobin in glycerolD(8)/D(2)O solution using incoherent elastic (ENS) and quasi-elastic (QENS) neutron scattering. Taking advantage of complementary energy resolutions of backscattering spectrometers at ILL (Grenoble), we explore motions in a large space-time window, up to 1 ns and 14 A; moreover, in order to cover the harmonic and anharmonic protein dynamics regimes, the elastic experiments have been performed over the wide temperature interval of 20-300 K. To study the dependence of the measured dynamics upon the protein quaternary structure, both deoxyhemoglobin (in T quaternary conformation) and carbonmonoxyhemoglobin (in R quater…

Quantitative Biology::BiomoleculesChemistryProtein dynamicsOrganic ChemistryNeutron diffractionMomentum transferAnharmonicityBiophysicsTemperatureProtein dynamicsHemoglobin quaternary structureMean square displacementDynamical transitionNeutron scatteringBiochemistryElasticityMean squared displacementOxygenHemoglobinsNeutron DiffractionHumansDiffusion (business)Atomic physicsStructure factorHydrogenBiophysical chemistry
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Dynamics of myoglobin in confinement: An elastic and quasi-elastic neutron scattering study

2008

In order to clarify the role of hard confinement on protein dynamics, elastic and quasi-elastic neutron scattering experiments have been performed on ferric horse myoglobin in two different systems: the protein embedded in a porous silica matrix, and the corresponding hydrated protein powder. Elastic data have been analysed using two different models (dynamical heterogeneity and anharmonic double-well potential) that take into account deviations of elastic intensity from Gaussian behaviour. The profile of quasi-elastic spectra has been approximated by a combination of Lorentzian and Gaussian components. Comparison between the data relative to the two different samples indicates that geometr…

GLASS-TRANSITIONGaussianGeneral Physics and AstronomyHydrationNeutron scatteringSol–gelMYELIN BASIC-PROTEINMolecular physicsSpectral linesymbols.namesakechemistry.chemical_compoundDynamical heterogeneityPhysical and Theoretical ChemistryPorosityHEMOGLOBINSOLVENTQuantitative Biology::BiomoleculesProtein dynamicsAnharmonicitySolvent dynamicCrystallographyMyoglobinchemistrysymbolsProtein dynamicSilica hydrogels
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Anomalous water dynamics in brain: a combined diffusion magnetic resonance imaging and neutron scattering investigation

2019

International audience; Water diffusion is an optimal tool for investigating the architecture of brain tissue on which modern medical diagnostic imaging techniques rely. However, intrinsic tissue heterogeneity causes systematic deviations from pure free-water diffusion behaviour. To date, numerous theoretical and empirical approaches have been proposed to explain the non-Gaussian profile of this process. The aim of this work is to shed light on the physics piloting water diffusion in brain tissue at the micrometre-to-atomic scale. Combined diffusion magnetic resonance imaging and first pioneering neutron scattering experiments on bovine brain tissue have been performed in order to probe dif…

Medical diagnosticMaterials science[SDV.IB.IMA]Life Sciences [q-bio]/Bioengineering/ImagingQuantitative Biology::Tissues and OrgansPhysics::Medical PhysicsBiomedical EngineeringBiophysicsproton dynamicsBioengineeringbrain imagingNeutron scatteringBiochemistryAtomic unitsBiomaterials03 medical and health sciences0302 clinical medicineTissue heterogeneityWater dynamicsNuclear magnetic resonancemedicineAnimalsDiffusion (business)030304 developmental biologydiffusion magnetic resonance imaging0303 health sciencesProton dynamicmedicine.diagnostic_testneutron scatteringBrainWaterMagnetic resonance imagingwater diffusionLife Sciences–Physics interfaceMagnetic Resonance ImagingSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Neutron Diffraction[SDV.IB.IMA] Life Sciences [q-bio]/Bioengineering/ImagingBovine brainBrain imaging; Diffusion magnetic resonance imaging; Neutron scattering; Proton dynamics; Water diffusionCattle030217 neurology & neurosurgeryBiotechnology
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Dynamical properties of water in living cells

2018

With the aim of studying the effect of water dynamics on the properties of biological systems, in this paper, we present a quasi-elastic neutron scattering study on three different types of living cells, differing both in their morphological and tumor properties. The measured scattering signal, which essentially originates from hydrogen atoms present in the investigated systems, has been analyzed using a global fitting strategy using an optimized theoretical model that considers various classes of hydrogen atoms and allows disentangling diffusive and rotational motions. The approach has been carefully validated by checking the reliability of the calculation of parameters and their 99% confi…

Properties of waterScale (ratio)HydrogenPhysics and Astronomy (miscellaneous)chemistry.chemical_elementNeutron scattering010402 general chemistrySpace (mathematics)01 natural sciencesSignalchemistry.chemical_compoundOpticsquasi-elastic neutron scatteringwater structure and dynamicintracellular water0103 physical sciences010306 general physicsintracellular water; quasi-elastic neutron scattering; water structure and dynamics; Physics and Astronomy (miscellaneous)Physicsbusiness.industryScatteringSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)0104 chemical scienceswater structure and dynamicschemistryPicosecondbusinessBiological system
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Mobility of a Mononucleotide within a Lipid Matrix: A Neutron Scattering Study

2017

International audience; An essential question in studies on the origins of life is how nucleic acids were first synthesized and then incorporated into compartments about 4 billion years ago. A recent discovery is that guided polymerization within organizing matrices could promote a non-enzymatic condensation reaction allowing the formation of RNA-like polymers, followed by encapsulation in lipid membranes. Here, we used neutron scattering and deuterium labelling to investigate 5'-adenosine monophosphate (AMP) molecules captured in a multilamellar phospholipid matrix. The aim of the research was to determine and compare how mononucleotides are captured and differently organized within matric…

0301 basic medicinemultilamellar lipid matrix[PHYS.PHYS.PHYS-BIO-PH]Physics [physics]/Physics [physics]/Biological Physics [physics.bio-ph]neutron scattering; multilamellar lipid matrix; mononucleotide mobility; hydrationPhospholipidNeutron scattering010402 general chemistry01 natural sciencesGeneral Biochemistry Genetics and Molecular BiologyArticle03 medical and health scienceschemistry.chemical_compoundMoleculelcsh:ScienceLipid bilayerEcology Evolution Behavior and Systematicschemistry.chemical_classification[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]neutron scatteringPaleontologyPolymer0104 chemical sciencesmononucleotide mobility[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM]030104 developmental biologyMembranechemistryBiochemistryDeuteriumPolymerizationSpace and Planetary ScienceChemical physicslcsh:Qlipids (amino acids peptides and proteins)hydration
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Molecular origin and hydration dependence of protein anharmonicity: an elastic neutron scattering study.

2010

Two main onsets of anharmonicity are present in protein dynamics. Neutron scattering on protein hydrated powders revealed a first onset at about 150 K and a second one at about 230 K (the so called dynamical transition). In order to assess the molecular origin of protein anharmonicity, we study different homomeric polypeptides by incoherent elastic neutron scattering, thus disentangling the contribution of different molecular groups in proteins. We show that methyl group rotations are the main contributors to the low temperature onset. Concerning the dynamical transition, we show that it also occurs in absence of side chains; however, the presence and mobility of side chains substantially i…

Elastic scatteringQuantitative Biology::BiomoleculespolypeptideTransition temperatureProtein dynamicsAnharmonicitymean square displacementsTemperatureGeneral Physics and AstronomyProteinsWaterNeutron scatteringElasticitychemistry.chemical_compoundCrystallographyNeutron DiffractionAmplitudechemistryChemical physicsprotein dynamicSide chainPhysics::Chemical PhysicsPhysical and Theoretical ChemistryPeptidesMethyl groupPhysical chemistry chemical physics : PCCP
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A benchmark for protein dynamics: Ribonuclease A measured by neutron scattering in a large wavevector-energy transfer range

2008

The dynamics of Ribonuclease A was explored in the full range of time and length-scales accessible by neutron spectroscopy, on time-of-flight, backscattering and spin-echo spectrometers. Samples were examined in dry and hydrated powder forms and in concentrated and dilute solutions. The aim of the study was an experimental characterisation of the full variety of protein dynamics arising from stabilisation forces. The results provide a benchmark against which other sample dynamics can be compared.

Quantitative Biology::BiomoleculesRange (particle radiation)SpectrometerChemistryProtein dynamicsDynamics (mechanics)General Physics and AstronomyNeutron scatteringMolecular physicsNeutron spectroscopyBenchmark (computing)Wave vectorPhysical and Theoretical ChemistryAtomic physicsChemical Physics
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Water Dynamics in Neural Tissue

2013

Water dynamics in post-mortem two-years old bovine cerebral right hemisphere has been investigated through Elastic and Quasi-elastic Neutron Scattering. Experimental parameters such as stability in time of the proton dynamics, data reproducibility and changes in the tissues dynamics upon the conservation protocol, cryogenic towards formalin addition, have been carefully investigated. Results are extremely encouraging and comparisons to magnetic resonance imaging findings are discussed.

ReproducibilityMaterials sciencemedicine.diagnostic_testProtonneutron scatteringDynamics (mechanics)proton dynamicsGeneral Physics and AstronomyMagnetic resonance imagingNeutron scatteringNuclear magnetic resonanceWater dynamicsmedicineRight hemispherediffusion magnetic resonance imagingJournal of the Physical Society of Japan
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The Boson Peak of Amyloid Fibrils: Probing the Softness of Protein Aggregates by Inelastic Neutron Scattering

2014

Proteins and polypeptides are characterized by low-frequency vibrations in the terahertz regime responsible for the so-called "boson peak". The shape and position of this peak are related to the mechanical properties of peptide chains. Amyloid fibrils are ordered macromolecular assemblies, spontaneously formed in nature, characterized by unique biological and nanomechanical properties. In this work, we investigate the effects of the amyloid state and its polymorphism on the boson peak. We used inelastic neutron scattering to probe low-frequency vibrations of the glucagon polypeptide in the native state and in two different amyloid morphologies in both dry and hydrated sample states. The dat…

AmyloidPhysics::Biological PhysicsQuantitative Biology::BiomoleculesChemistryProtein dynamicsNeutron diffractionNeutron scatteringProtein aggregationFibrilVibrationAmyloid Protein dynamics collective motions boson peakInelastic neutron scatteringSurfaces Coatings and FilmsNeutron DiffractionMicroscopy Electron TransmissionChemical physicsMolecular vibrationSpectroscopy Fourier Transform InfraredMaterials ChemistryNative statePhysical and Theoretical ChemistryAtomic physics
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Erratum to: Dynamical properties of water in living cells (Front. Phys, (2018) 13, 1, 138301, 10.1007/s11467-017-0731-5)

2018

In the original publication of the article, the label Q2(A-2) in Fig. 4 should be replaced with Q(A-1). Below is the correct Fig. 4.[Figure not available: see fulltext.]. © 2018, Higher Education Press and Springer-Verlag GmbH Germany, part of Springer Nature.

Physics and Astronomy (miscellaneous)-Settore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)
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