RESUMEN
Scattering techniques represent non-invasive experimental approaches and powerful tools for the investigation of structure and conformation of biomaterial systems in a wide range of distances, ranging from the nanometric to micrometric scale. More specifically, small-angle X-rays and neutron scattering and light scattering techniques represent well-established experimental techniques for the investigation of the structural properties of biomaterials and, through the use of suitable models, they allow to study and mimic various biological systems under physiologically relevant conditions. They provide the ensemble averaged (and then statistically relevant) information under in situ and operando conditions, and represent useful tools complementary to the various traditional imaging techniques that, on the contrary, reveal more local structural information. Together with the classical structure characterization approaches, we introduce the basic concepts that make it possible to examine inter-particles interactions, and to study the growth processes and conformational changes in nanostructures, which have become increasingly relevant for an accurate understanding and prediction of various mechanisms in the fields of biotechnology and nanotechnology. The upgrade of the various scattering techniques, such as the contrast variation or time resolved experiments, offers unique opportunities to study the nano- and mesoscopic structure and their evolution with time in a way not accessible by other techniques. For this reason, highly performant instruments are installed at most of the facility research centers worldwide. These new insights allow to largely ameliorate the control of (chemico-physical and biologic) processes of complex (bio-)materials at the molecular length scales, and open a full potential for the development and engineering of a variety of nano-scale biomaterials for advanced applications.
Asunto(s)
Materiales Biocompatibles/química , Dispersión Dinámica de Luz/métodos , Difracción de Neutrones/métodos , Dispersión del Ángulo Pequeño , Difracción de Rayos X/métodos , Materiales Biocompatibles/metabolismo , Dispersión Dinámica de Luz/instrumentación , Difracción de Neutrones/instrumentación , Relación Estructura-Actividad , Difracción de Rayos X/instrumentaciónRESUMEN
Neutron diffraction is exquisitely sensitive to the positions of H atoms in protein crystal structures. IMAGINE is a high-intensity, quasi-Laue neutron crystallography beamline developed at the High Flux Isotope Reactor (HFIR) at Oak Ridge National Laboratory. This state-of-the-art facility for neutron diffraction has enabled detailed structural analysis of macromolecules. IMAGINE is especially suited to resolve individual H atoms in protein structures, enabling neutron protein structures to be determined at or near atomic resolutions from crystals with volumes of less than 1â mm3 and unit-cell edges of less than 150â Å. Beamline features include elliptical focusing mirrors that deliver neutrons into a 2.0 × 3.2â mm focal spot at the sample position, and variable short- and long-wavelength cutoff optics that provide automated exchange between multiple wavelength configurations. This review gives an overview of the IMAGINE beamline at the HFIR, presents examples of the scientific questions being addressed at this beamline, and highlights important findings in enzyme chemistry that have been made using the neutron diffraction capabilities offered by IMAGINE.
Asunto(s)
Enzimas/química , Difracción de Neutrones/instrumentación , Cristalografía , Deuterio , Hidrógeno , Difracción de Neutrones/métodosRESUMEN
Hybrid self-assembling nanoparticles (hsaNPs) encapsulating bisphosphonates (BPs) recently showed very promising results in preclinic experiments for the treatment of brain tumor. However, the poor knowledge on the architecture of hybrid nanovectors is certainly one of the main reasons hampering further clinical and industrial development of these technologies. Here we propose to combine different techniques, that is, small angle neutron scattering (SANS) and X-ray Sscattering (SAXS), with cryo-electron transmission microscopy (cryo-TEM) to study the architecture of the final hsaNPs as well as of the four components before the assembling process. Data analysis based on SANS and SAXS experiments suggested a multiple compartment architecture of the final product, consisting of two bilayers sourrounding a core. Structures consisting of two shells surrounding an internal core were also observed in the cryo-TEM analysis. Such high resolution insight, also combined with size distribution and zeta potential of the NPs, provides exhaustive characterization of hsaNPs encapsulating BPs, and it is aimed at supporting further their clinical and industrial development.
Asunto(s)
Antineoplásicos/administración & dosificación , Composición de Medicamentos/métodos , Nanopartículas/química , Neoplasias/tratamiento farmacológico , Ácido Zoledrónico/administración & dosificación , Microscopía por Crioelectrón , Ácidos Grasos Monoinsaturados/química , Humanos , Liposomas , Microscopía Electrónica de Transmisión , Estructura Molecular , Nanopartículas/ultraestructura , Difracción de Neutrones/instrumentación , Difracción de Neutrones/métodos , Fosfatidiletanolaminas/química , Polietilenglicoles/química , Compuestos de Amonio Cuaternario/química , Dispersión del Ángulo Pequeño , Transferrina/química , Difracción de Rayos X/instrumentación , Difracción de Rayos X/métodosRESUMEN
Small-angle neutron scattering (SANS) is maturing as a method for studying complex biological structures. Owing to the intrinsic ability of the technique to discern between 1H- and 2H-labelled particles, it is especially useful for contrast-variation studies of biological systems containing multiple components. SANS is complementary to small-angle X-ray scattering (SAXS), in which similar contrast variation is not easily performed but in which data with superior counting statistics are more easily obtained. Obtaining small-angle scattering (SAS) data on monodisperse complex biological structures is often challenging owing to sample degradation and/or aggregation. This problem is enhanced in the D2O-based buffers that are typically used in SANS. In SAXS, such problems are solved using an online size-exclusion chromatography (SEC) setup. In the present work, the feasibility of SEC-SANS was investigated using a series of complex and difficult samples of membrane proteins embedded in nanodisc particles that consist of both phospholipid and protein components. It is demonstrated that SEC-SANS provides data of sufficient signal-to-noise ratio for these systems, while at the same time circumventing aggregation. By combining SEC-SANS and SEC-SAXS data, an optimized basis for refining structural models of the investigated structures is obtained.
Asunto(s)
Proteínas Bacterianas/química , Proteínas de Transporte de Catión/química , Difracción de Neutrones/métodos , Fosfolípidos/química , Dispersión del Ángulo Pequeño , Thermotoga maritima/química , Cromatografía en Gel , Diseño de Equipo , Nanoestructuras/química , Difracción de Neutrones/instrumentación , Difracción de Rayos XRESUMEN
Clarification of solution structure and its modulation in proteins and protein complexes is crucially important to understand dynamical ordering in macromolecular systems. Small-angle x-ray scattering (SAXS) and small-angle neutron scattering (SANS) are among the most powerful techniques to derive structural information. Recent progress in sample preparation, instruments and software analysis is opening up a new era for small-angle scattering. In this review, recent progress and trends of SAXS and SANS are introduced from the point of view of instrumentation and analysis, touching on general features and standard methods of small-angle scattering. This article is part of a Special Issue entitled "Biophysical Exploration of Dynamical Ordering of Biomolecular Systems" edited by Dr. Koichi Kato.
Asunto(s)
Biología Computacional , Modelos Biológicos , Difracción de Neutrones , Proteínas/metabolismo , Dispersión del Ángulo Pequeño , Difracción de Rayos X , Animales , Diseño de Equipo , Humanos , Cinética , Simulación de Dinámica Molecular , Difracción de Neutrones/instrumentación , Conformación Proteica , Proteínas/química , Relación Estructura-Actividad , Difracción de Rayos X/instrumentaciónRESUMEN
Small angle scattering (SAS) is a powerful and versatile tool to elucidate the structure of matter at the nanometer scale. Recently, the technique has seen a tremendous growth of applications in the field of structural molecular biology. Its origins however date back to almost a century ago and even though the methods potential for studying biological macromolecules was realized already early on, it was only during the last two decades that SAS gradually became a major experimental technique for the structural biologist. This rise in popularity and application was driven by the concurrence of different key factors such as the increased accessibility to high quality SAS instruments enabled by the growing number of synchrotron facilities and neutron sources established around the world, the emerging need of the structural biology community to study large multi-domain complexes and flexible systems that are hard to crystalize, and in particular the development and availability of data analysis software together with the overall access to computational resources powerful enough to run them. Today, SAS is an established and widely used tool for structural studies on bio-macromolecules. Given the potential offered by the next generation X-ray and neutron sources as well as the development of new, innovative approaches to collect and analyze solution scattering data, the application of SAS in the field of structural molecular biology will certainly continue to thrive in the years to come.
Asunto(s)
Biología Molecular/historia , Difracción de Neutrones/historia , Dispersión del Ángulo Pequeño , Difracción de Rayos X/historia , Historia del Siglo XX , Historia del Siglo XXI , Humanos , Biología Molecular/instrumentación , Biología Molecular/métodos , Biología Molecular/tendencias , Difracción de Neutrones/instrumentación , Difracción de Neutrones/métodos , Sincrotrones/historia , Sincrotrones/instrumentación , Difracción de Rayos X/instrumentación , Difracción de Rayos X/métodosRESUMEN
Solution small-angle neutron scattering (SANS) combined with contrast variation provides information about the size and shape of individual components of a multi-component biological assembly, as well as the spatial arrangements between the components. The large difference in the neutron scattering properties between hydrogen and deuterium is key to the method. Isotopic substitution of deuterium for some or all of the hydrogen in either the molecule or the solvent can greatly alter the scattering properties of the biological assembly, often with little or no change to its biochemical properties. Thus, SANS with contrast variation provides unique information not easily obtained using other experimental techniques.If used correctly, SANS with contrast variation is a powerful tool for determining the solution structure of multi-component biological assemblies. This chapter discusses the principles of SANS theory that are important for contrast variation, essential considerations for experiment design and execution, and the proper approach to data analysis and structure modeling. As sample quality is extremely important for a successful contrast variation experiment, sample issues that can affect the outcome of the experiment are discussed as well as procedures used to verify the sample quality. The described methodology is focused on two-component biological complexes. However, examples of its use for multi-component assemblies are also discussed.
Asunto(s)
Medición de Intercambio de Deuterio/métodos , Difracción de Neutrones/métodos , Ácidos Nucleicos/ultraestructura , Proteínas/ultraestructura , Dispersión del Ángulo Pequeño , Simulación por Computador , Exactitud de los Datos , Deuterio/química , Humanos , Hidrógeno/química , Modelos Moleculares , Conformación Molecular , Difracción de Neutrones/instrumentación , Ácidos Nucleicos/química , Proteínas/química , Proyectos de InvestigaciónRESUMEN
Intrinsically Disordered Proteins (IDPs) are fundamental actors of biological processes. Their inherent plasticity facilitates very specialized tasks in cell regulation and signalling, and their malfunction is linked to severe pathologies. Understanding the functional role of disorder requires the structural characterization of IDPs and the complexes they form. Small-angle Scattering of X-rays (SAXS) and Neutrons (SANS) have notably contributed to this structural understanding. In this review we summarize the most relevant developments in the field of SAS studies of disordered proteins. Emphasis is given to ensemble methods and how SAS data can be combined with computational approaches or other biophysical information such as NMR. The unique capabilities of SAS enable its application to extremely challenging disordered systems such as low-complexity regions, amyloidogenic proteins and transient biomolecular complexes. This reinforces the fundamental role of SAS in the structural and dynamic characterization of this elusive family of proteins.
Asunto(s)
Proteínas Amiloidogénicas/ultraestructura , Proteínas Intrínsecamente Desordenadas/ultraestructura , Modelos Moleculares , Dispersión del Ángulo Pequeño , Proteínas Amiloidogénicas/química , Simulación por Computador , Humanos , Proteínas Intrínsecamente Desordenadas/química , Difracción de Neutrones/instrumentación , Difracción de Neutrones/métodos , Resonancia Magnética Nuclear Biomolecular , Conformación Proteica , Sincrotrones/instrumentación , Difracción de Rayos X/instrumentación , Difracción de Rayos X/métodosRESUMEN
Small angle scattering of X-rays (SAXS) and neutrons (SANS) is a structural technique to study disordered systems with chaotic orientations of scattering inhomogeneities at low resolution. An important example of such systems are solutions of biological macromolecules. Rapid development in the methodology for solution scattering data interpretation and model building during the last two decades brought the analysis far beyond the determination of just few overall structural parameters (which was the only possibility in the past) and ensured SAS a firm position in the methods palette of the modern life sciences. The advances in the methodology include ab initio approaches for shape and domain structure restoration from scattering curves without a priori structural knowledge, classification and validation of the models, evaluation of potential ambiguity associated with the reconstruction. In rigid body and hybrid modelling approaches, solution scattering is synergistically used with other structural techniques utilizing the complementary information such as atomic models of the components, intramolecular contacts, subunits orientations etc. for the reconstruction of complex systems. The usual requirement of the sample monodispersity has been loosed recently and the technique can now address such systems as weakly bound oligomers and transient complexes. These state-of-the-art methods are described together with the examples of their applications and the possible ways of post-processing of the models.
Asunto(s)
Modelos Moleculares , Ácidos Nucleicos/ultraestructura , Proteínas/ultraestructura , Dispersión del Ángulo Pequeño , Simulación por Computador , Interpretación Estadística de Datos , Humanos , Conformación Molecular , Difracción de Neutrones/instrumentación , Difracción de Neutrones/métodos , Ácidos Nucleicos/química , Proteínas/química , Sincrotrones/instrumentación , Difracción de Rayos X/instrumentación , Difracción de Rayos X/métodosRESUMEN
Extending collection of x-ray solution scattering data into the wide-angle regime (WAXS) can provide information not readily extracted from small angle (SAXS) data. It is possible to accurately predict WAXS scattering on the basis of atomic coordinate sets and thus use it as a means of testing molecular models constructed on the basis of crystallography, molecular dynamics (MD), cryo-electron microscopy or ab initio modeling. WAXS data may provide insights into the secondary, tertiary and quaternary structural organization of macromolecules. It can provide information on protein folding and unfolding beyond that attainable from SAXS data. It is particularly sensitive to structural fluctuations in macromolecules and can be used to generate information about the conformational make up of ensembles of structures co-existing in solution. Novel approaches to modeling of structural fluctuations can provide information on the spatial extent of large-scale structural fluctuations that are difficult to obtain by other means. Direct comparison with the results of MD simulations are becoming possible. Because it is particularly sensitive to small changes in structure and flexibility it provides unique capabilities for the screening of ligand libraries for detection of functional interactions. WAXS thereby provides an important extension of SAXS that can generate structural and dynamic information complementary to that obtainable by other biophysical techniques.
Asunto(s)
Simulación de Dinámica Molecular , Proteínas/ultraestructura , Difracción de Rayos X/métodos , Microscopía por Crioelectrón/métodos , Cristalografía por Rayos X/métodos , Humanos , Difracción de Neutrones/instrumentación , Difracción de Neutrones/métodos , Conformación Proteica , Pliegue de Proteína , Proteínas/química , Dispersión del Ángulo Pequeño , Homología Estructural de Proteína , Difracción de Rayos X/instrumentaciónRESUMEN
Measuring distances within or between macromolecules is necessary to understand the chemistry that biological systems uniquely enable. In performing their chemistry, biological macromolecules undergo structural changes over distances ranging from atomic to micrometer scales. X-ray and neutron scattering provide three key assets for tackling this challenge. First, they may be conducted on solutions where the macromolecules are free to sample the conformations that enable their chemistry. Second, there are few limitations on chemical environment for experiments. Third, the techniques can inform upon a wide range of distances at once. Thus scattering, particularly recorded at small angles (SAS), has been applied to a large variety of phenomenon. A challenge in interpreting scattering data is that the desired three dimensional distance information is averaged onto one dimension. Furthermore, the scales and variety of phenomenon interrogated have led to an assortment of functions that describe distances and changes thereof. Here we review scattering studies that characterize biological phenomenon at distances ranging from atomic to 50 nm. We also distinguish the distance distribution functions that are commonly used to describe results from these systems. With available X-ray and neutron scattering facilities, bringing the action that occurs at the atomic to the micrometer scale is now reasonably accessible. Notably, the combined distance and dynamic information recorded by SAS is frequently key to connecting structure to biological activity and to improve macromolecular design strategies and outcomes. We anticipate widespread utilization particularly in macromolecular engineering and time-resolved studies where many contrasting experiments are necessary for resolving chemical mechanisms through structural changes.
Asunto(s)
Modelos Moleculares , Proteínas/ultraestructura , Coloración y Etiquetado/métodos , Difracción de Rayos X/métodos , Espectroscopía de Resonancia por Spin del Electrón , Transferencia Resonante de Energía de Fluorescencia , Oro/química , Humanos , Lípidos/química , Difracción de Neutrones/instrumentación , Difracción de Neutrones/métodos , Conformación Proteica , Proteínas/química , Dispersión del Ángulo Pequeño , Soluciones , Agua/química , Difracción de Rayos X/instrumentaciónRESUMEN
Biomolecular applications of solution X-ray and neutron scattering (SAXS and SANS, respectively) started in late 1960s - early 1970s but were relatively limited in their ability to provide a detailed structural picture and lagged behind what became the two primary methods of experimental structural biology - X-ray crystallography and NMR. However, improvements in both data analysis and instrumentation led to an explosive growth in the number of studies that used small-angle scattering (SAS) for investigation of macromolecular structure, often in combination with other biophysical techniques. Such hybrid applications are nowadays quickly becoming a norm whenever scattering data are used for two reasons. First, it is generally accepted that SAS data on their own cannot lead to a uniquely defined high-resolution structural model, creating a need for supplementing them with information from complementary techniques. Second, solution scattering data are frequently applied in situations when a method such NMR or X-ray crystallography cannot provide a satisfactory structural picture, which makes these additional restraints highly desirable. Maturation of the hybrid bio-SAS approaches brings to light new questions including completeness of the conformational space sampling, model validation, and data compatibility.
Asunto(s)
Cristalografía por Rayos X/métodos , Resonancia Magnética Nuclear Biomolecular/métodos , Proteínas/ultraestructura , ARN/ultraestructura , Dispersión del Ángulo Pequeño , Sincrotrones/instrumentación , Simulación por Computador , Cristalografía por Rayos X/instrumentación , Humanos , Modelos Moleculares , Conformación Molecular , Difracción de Neutrones/instrumentación , Difracción de Neutrones/métodos , Resonancia Magnética Nuclear Biomolecular/instrumentación , Proteínas/química , ARN/química , Difracción de Rayos X/instrumentación , Difracción de Rayos X/métodosRESUMEN
Small angle neutron scattering (SANS) is a powerful tool to obtain structural information on solubilized membrane proteins on the nanometer length-scale in complement to other structural biology techniques such as cryo-EM, NMR and SAXS. In combination with deuteration of components and/or contrast variation (H2O:D2O exchange in the buffer) SANS allows to separate structural information from the protein and the detergent/lipid parts in solution. After a short historical overview on results obtained by SANS on membrane protein systems, this book chapter introduces the basic theoretical principles of the technique as well as requirements on samples. The two introductory sections are followed by an illustration of the specific consequences of sample heterogeneity of solubilized membrane proteins in the presence of detergent/lipid molecules on the interpretation of structural information by using simple, geometric models. The next sections deal with more sophisticated modelling approaches including ab initio shape reconstructions and full-atomic models in the presence of detergent/lipid and specific results obtained by these approaches. After a short comparison with the SAXS technique, this book chapter concludes with an overview of present and future developments and impact that can be expected by SANS on membrane structural biology in the coming years.
Asunto(s)
Medición de Intercambio de Deuterio/métodos , Proteínas de la Membrana/ultraestructura , Dispersión del Ángulo Pequeño , Manejo de Especímenes/métodos , Sincrotrones/instrumentación , Tampones (Química) , Simulación por Computador , Detergentes/química , Humanos , Lípidos/química , Proteínas de la Membrana/química , Modelos Moleculares , Difracción de Neutrones/instrumentación , Difracción de Neutrones/métodos , Conformación Proteica , Difracción de Rayos X/instrumentación , Difracción de Rayos X/métodosRESUMEN
The sub-nanometer scale provided by small angle neutron and X-ray scattering is of special importance to pharmaceutical and biomedical investigators. As drug delivery devices become more functionalized and continue decreasing in size, the ability to elucidate details on size scales smaller than those available from optical techniques becomes extremely pertinent. Information gathered from small angle scattering therefore aids the endeavor of optimizing pharmaceutical efficacy at its most fundamental level. This chapter will provide some relevant examples of drug carrier technology and how small angle scattering (SAS) can be used to solve their mysteries. An emphasis on common first-step data treatments is provided which should help clarify the contents of scattering data to new researchers. Specific examples of pharmaceutically relevant research on novel systems and the role SAS plays in these studies will be discussed. This chapter provides an overview of the current applications of SAS in drug research and some practical considerations for selecting scattering techniques.
Asunto(s)
Cápsulas/química , Sistemas de Liberación de Medicamentos/métodos , Drogas en Investigación/química , Nanopartículas/química , Dispersión del Ángulo Pequeño , Animales , Recolección de Datos/estadística & datos numéricos , Interpretación Estadística de Datos , Humanos , Micelas , Conformación Molecular , Nanopartículas/ultraestructura , Difracción de Neutrones/instrumentación , Difracción de Neutrones/métodos , Difracción de Rayos X/instrumentación , Difracción de Rayos X/métodosRESUMEN
A procedure for the operation of a new dielectric RheoSANS instrument capable of simultaneous interrogation of the electrical, mechanical and microstructural properties of complex fluids is presented. The instrument consists of a Couette geometry contained within a modified forced convection oven mounted on a commercial rheometer. This instrument is available for use on the small angle neutron scattering (SANS) beamlines at the National Institute of Standards and Technology (NIST) Center for Neutron Research (NCNR). The Couette geometry is machined to be transparent to neutrons and provides for measurement of the electrical properties and microstructural properties of a sample confined between titanium cylinders while the sample undergoes arbitrary deformation. Synchronization of these measurements is enabled through the use of a customizable program that monitors and controls the execution of predetermined experimental protocols. Described here is a protocol to perform a flow sweep experiment where the shear rate is logarithmically stepped from a maximum value to a minimum value holding at each step for a specified period of time while frequency dependent dielectric measurements are made. Representative results are shown from a sample consisting of a gel composed of carbon black aggregates dispersed in propylene carbonate. As the gel undergoes steady shear, the carbon black network is mechanically deformed, which causes an initial decrease in conductivity associated with the breaking of bonds comprising the carbon black network. However, at higher shear rates, the conductivity recovers associated with the onset of shear thickening. Overall, these results demonstrate the utility of the simultaneous measurement of the rheo-electro-microstructural properties of these suspensions using the dielectric RheoSANS geometry.
Asunto(s)
Impedancia Eléctrica , Difracción de Neutrones/instrumentación , Reología/instrumentación , Dispersión del Ángulo Pequeño , Suspensiones , Factores de TiempoRESUMEN
J-PARC, Japan Proton Accelerator Research Complex provides short pulse proton beam at a repetition rate 25Hz and the maximum power is expected to be 1MW. Materials and Life Science Experimental Facility (MLF) has 23 neutron beam ports and 21 instruments have already been operated or under construction/commissioning. There are 6 inelastic/quasi-elastic neutron scattering spectrometers and the complementary use of these spectrometers will open new insight for life science. This article is part of a Special Issue entitled "Science for Life" Guest Editor: Dr. Austen Angell, Dr. Salvatore Magazù and Dr. Federica Migliardo.
Asunto(s)
Elasticidad , Difracción de Neutrones/instrumentación , Análisis Espectral/instrumentación , ADN/química , Japón , Membrana Dobles de Lípidos/química , Fonones , Protones , Agua/químicaRESUMEN
We present an upgrade to the time-of-flight neutron reflectometer BioRef at the research reactor BER II of the Helmholtz-Zentrum Berlin für Materialien und Energie (HZB). Through the integration of an additional chopper into the existing setup, the available wavelength resolution is significantly extended. Now two distinct operation modes can be used: a high resolution mode with Δλ/λ ranging from 1% to 5%, which allows for the investigation of thick films up to 4000 Å, and a high flux mode with Δλ/λ = 7%-11%. In the high flux mode, reflectivity curves from 0.007 Å-1 to 0.2 Å-1 with three angular settings can be recorded in 7 min. For a single angular setting and its respective window in Q-space, a time resolution of even less than 4 min is reached. The different configurations are documented by respective measurements (a) on a Ni-Ti multilayer and (b) the swelling kinetics of a solid-supported phospholipid coating upon incubation in a polyelectrolyte solution.
Asunto(s)
Modelos Teóricos , Difracción de Neutrones , Dispersión de Radiación , Difracción de Neutrones/instrumentación , Difracción de Neutrones/métodosRESUMEN
We have designed and constructed a temperature-controllable shear flow cell for in-situ study on flow alignable systems. The device has been tested in the neutron diffraction and has the potential to be applied in the small angle neutron scattering configuration to characterize the nanostructures of the materials under flow. The required sample amount is as small as 1 ml. The shear rate on the sample is controlled by the flow rate produced by an external pump and can potentially vary from 0.11 to 3.8 × 10(5) s(-1). Both unidirectional and oscillational flows are achievable by the setting of the pump. The instrument is validated by using a lipid bicellar mixture, which yields non-alignable nanodisc-like bicelles at low T and shear-alignable membranes at high T. Using the shear cell, the bicellar membranes can be aligned at 31 °C under the flow with a shear rate of 11.11 s(-1). Multiple high-order Bragg peaks are observed and the full width at half maximum of the "rocking curve" around the Bragg's condition is found to be 3.5°-4.1°. It is noteworthy that a portion of the membranes remains aligned even after the flow stops. Detailed and comprehensive intensity correction for the rocking curve has been derived based on the finite rectangular sample geometry and the absorption of the neutrons as a function of sample angle [See supplementary material at http://dx.doi.org/10.1063/1.4908165 for the detailed derivation of the absorption correction]. The device offers a new capability to study the conformational or orientational anisotropy of the solvated macromolecules or aggregates induced by the hydrodynamic interaction in a flow field.
Asunto(s)
Fenómenos Mecánicos , Micelas , Difracción de Neutrones/instrumentación , Temperatura , Glicerofosfolípidos/química , Hidrodinámica , Análisis EspectralRESUMEN
Li-ion batteries are widely used in portable electronic devices and are considered as promising candidates for higher-energy applications such as electric vehicles. However, many challenges, such as energy density and battery lifetimes, need to be overcome before this particular battery technology can be widely implemented in such applications. This research is challenging, and we outline a method to address these challenges using in situ NPD to probe the crystal structure of electrodes undergoing electrochemical cycling (charge/discharge) in a battery. NPD data help determine the underlying structural mechanism responsible for a range of electrode properties, and this information can direct the development of better electrodes and batteries. We briefly review six types of battery designs custom-made for NPD experiments and detail the method to construct the 'roll-over' cell that we have successfully used on the high-intensity NPD instrument, WOMBAT, at the Australian Nuclear Science and Technology Organisation (ANSTO). The design considerations and materials used for cell construction are discussed in conjunction with aspects of the actual in situ NPD experiment and initial directions are presented on how to analyze such complex in situ data.