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1.
J Synchrotron Radiat ; 22(3): 508-13, 2015 May.
Artigo em Inglês | MEDLINE | ID: mdl-25931061

RESUMO

The X-ray Correlation Spectroscopy instrument is dedicated to the study of dynamics in condensed matter systems using the unique coherence properties of free-electron lasers. It covers a photon energy range of 4-25 keV. The intrinsic temporal characteristics of the Linac Coherent Light Source, in particular the 120 Hz repetition rate, allow for the investigation of slow dynamics (milliseconds) by means of X-ray photon correlation spectroscopy. Double-pulse schemes could probe dynamics on the picosecond timescale. A description of the instrument capabilities and recent achievements is presented.

2.
J Synchrotron Radiat ; 21(Pt 6): 1288-95, 2014 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-25343797

RESUMO

A new approach is proposed for measuring structural dynamics in materials from multi-speckle scattering patterns obtained with partially coherent X-rays. Coherent X-ray scattering is already widely used at high-brightness synchrotron lightsources to measure dynamics using X-ray photon correlation spectroscopy, but in many situations this experimental approach based on recording long series of images (i.e. movies) is either not adequate or not practical. Following the development of visible-light speckle visibility spectroscopy, the dynamic information is obtained instead by analyzing the photon statistics and calculating the speckle contrast in single scattering patterns. This quantity, also referred to as the speckle visibility, is determined by the properties of the partially coherent beam and other experimental parameters, as well as the internal motions in the sample (dynamics). As a case study, Brownian dynamics in a low-density colloidal suspension is measured and an excellent agreement is found between correlation functions measured by X-ray photon correlation spectroscopy and the decay in speckle visibility with integration time obtained from the analysis presented here.

3.
Rev Sci Instrum ; 82(2): 025109, 2011 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-21361635

RESUMO

A low temperature sample environment for x-ray photon correlation spectroscopy measurements in small-angle scattering geometry is presented. The chamber has been designed to allow investigations of dynamical phenomena in supercooled liquids and the typical working temperature range is 110-330 K with a thermal stability ΔT/T down to 10(-4). A variable external magnetic field up to 0.12 T can be applied, which is of interest in studies of, e.g., ferrofluids and liquid crystalline materials. Here, technical details about the sample environment are given together with examples of recent applications.

4.
Phys Chem Chem Phys ; 12(35): 10215-20, 2010 Sep 21.
Artigo em Inglês | MEDLINE | ID: mdl-20668739

RESUMO

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 increases the fluctuations amplitude without influencing the transition temperature. We also investigate the role of hydration on the anharmonic contributions. Our study shows that methyl group rotations are unaffected by hydration and confirms that the dynamical transition is suppressed in dry samples. In hydrated samples, while the pure backbone contribution does not depend on the hydration h at h > or = 0.2, in the presence of side chains the anharmonic fluctuations involved in the dynamical transition are enhanced by increasing the water content.


Assuntos
Elasticidade , Difração de Nêutrons , Proteínas/química , Água/química , Peptídeos/química , Temperatura
5.
J Am Chem Soc ; 132(4): 1371-6, 2010 Feb 03.
Artigo em Inglês | MEDLINE | ID: mdl-20067251

RESUMO

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 time window of the spectrometer used; however, contributions on the order of 10-20% from the motions of other groups (e.g., the phenolic ring and the methylene groups) are present. Our data also indicate that the dynamical transition occurring at approximately 230 K can be attributed, at least at the hydration level investigated, mainly to motions involving backbone fluctuations.


Assuntos
Aminoácidos/química , Peptídeos/química , Proteínas/química , Simulação de Dinâmica Molecular , Mioglobina/química , Estrutura Secundária de Proteína
6.
Phys Rev E Stat Nonlin Soft Matter Phys ; 82(3 Pt 1): 031804, 2010 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-21230098

RESUMO

We report the results of x-ray photon correlation spectroscopy (XPCS) experiments on multilayers of a photosensitive azo-polymer which can be softened by photoisomerization. Time correlation functions have been measured at different temperatures and momentum transfers (q) and under different illumination conditions (dark, UV or visible). The correlation functions are well described by the Kohlrausch-Williams-Watts (KWW) form with relaxation times that are proportional to q(-1). The characteristic relaxation times follow the same Vogel-Fulcher-Tammann law describing the bulk viscosity of this polymer. The out-of-equilibrium relaxation dynamics following a UV photoperturbation are accelerated, which is in agreement with a fluidification effect previously measured by rheology. The transient dynamics are characterized by two times correlation function, and dynamical heterogeneity is evidenced by calculating the variance χ of the degree of correlation as a function of ageing time. A clear peak in χ appears at a well defined time τ(C) which scales with q(-1) and with the ageing time, in a similar fashion as previously reported in colloidal suspensions [O. Dauchot, Phys. Rev. Lett. 95, 265701 (2005)]. From an accurate analysis of the correlation functions we could demonstrate a temperature and light dependent cross-over from compressed KWW to simple exponential behavior.

7.
Phys Rev Lett ; 100(5): 055702, 2008 Feb 08.
Artigo em Inglês | MEDLINE | ID: mdl-18352390

RESUMO

The dynamic properties of nanoparticles suspended in a supercooled glass forming liquid are studied by x-ray photon correlation spectroscopy. While at high temperatures the particles undergo Brownian motion the measurements closer to the glass transition indicate hyperdiffusive behavior. In this state the dynamics is independent of the local structural arrangement of nanoparticles, suggesting a cooperative behavior governed by the near-vitreous solvent.

8.
Biophys Chem ; 116(3): 219-25, 2005 Aug 01.
Artigo em Inglês | MEDLINE | ID: mdl-15908102

RESUMO

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 quaternary conformation) have been investigated. From the ENS data the mean square displacements of the non-exchangeable hydrogen atoms of the protein and their temperature dependence are obtained. In agreement with previous results on hydrated powders, a dynamical transition at about 220 K is detected. The results show interesting differences between the two hemoglobin quaternary conformations, the T-state protein appearing more rigid and performing faster motions than the R-state one; however, these differences involve motions occurring in the nanosecond time scale and are not detected when only faster atomic motions in the time scale up to 100 ps are investigated. The QENS results put in evidence a relevant Lorentzian quasi-elastic contribution. Analysis of the dependence of the Elastic Incoherent Structure Factor (EISF) and of the Lorentzian halfwidth upon the momentum transfer suggests that the above quasi-elastic contribution arises from the diffusion inside a confined space, values of confinement radius and local diffusion coefficient being compatible with motions of hydrogen atoms of the amino acid side chains. When averaged over the whole range of momentum transfer the QENS data put in evidence differences between deoxy and carbonmonoxy hemoglobin and confirm the quaternary structure dependence of the protein dynamics in the nanosecond time scale.


Assuntos
Hemoglobinas/química , Difração de Nêutrons , Elasticidade , Humanos , Hidrogênio/química , Oxigênio/química , Temperatura
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