Search results for "Dynamical transition"
showing 10 items of 10 documents
The effect of water on protein dynamics
2004
Neutron diffraction and spectroscopy were applied to describe the hydration and dynamics of a soluble protein and a natural membrane from extreme halophilic Archaea. The quantitative dependence of protein motions on water activity was clearly illustrated, and it was established that a minimum hydration shell is required for the systems to access their functional resilience, i.e. a dynamics state that allows biological activity.
Dynamics of homomeric polypeptides studied with neutron scattering, dielectric spectroscopy and calorimetry
2012
Dynamical properties of myoglobin in an ultraviscous water-glycerol solvent investigated with elastic neutron scattering and FTIR spectroscopy
2018
Abstract Proteins have distinctive dynamical properties, characterized by the fluctuations of protein molecules among the different minima of their energy landscape. These fluctuations, progressively activated for temperature values larger than ~180 K, lead to a steep increase in the temperature dependence of all measurable dynamical properties. This phenomenon is known as Protein Dynamical Transition and, in spite of the intense studies due to its importance in protein function and to the relation with the fascinating fundamental thermodynamics of complex systems, many aspects of it are not yet clearly understood. Among these, the relationship with the properties of the external solvent an…
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 …
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…
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…
Dynamics and toxicity of proteins with a high homology of sequences: approach by molecular dynamics and ab-initio calculations
2008
The elucidation of the structure and the biological function of proteins is a major stake for its implications in the biomedical research as well as in biotechnologies. In addition, there is a glass or dynamical transition for the proteins which occurs at around 200K: it has been observed by Neutron Scattering, X-ray diffraction and Mossbauer spectroscopy for different proteins. Above the transition temperature, the biological function is activated as the protein may diffuse between conformational sub-states. The microscopic origin of this transition is still debated in spite of significant advances in recent years showing the significant role of hydration. By using all-atoms classical mole…
Anharmonic onsets in polypeptides revealed by neutron scattering: experimental ecidences and quantitative description of energy resolution dependence
2012
Supercooled Water Confined in a Silica Xerogel: Temperature and Pressure Dependence of Boson Peak and of Mean Square Displacements
2013
A silica xerogel can be obtained from an alcoxide precursor (TMOS, tetramethylortosilcate) via the sol-gel method: TMOS hydrolysis and subsequent polycondensation yields a solid, disordered, porous SiO2 matrix (average pore dimensions ~20Å). Inside the pores water is trapped and the hydration level h=gr[H2O]/gr[SiO2] can be easily controlled. The presence and temperature dependence of the boson peak (BP) in xerogel confined supercooled water was studied with inelastic neutron scattering (spectrometer IN6 at ILL, Grenoble) in xerogel samples having h=0.4 and h=0.2. After careful subtraction of the contributions arising from the matrix and from quasi-elastic scattering, the BP contribution wa…