SEARCH · PubMed Health

Results for “Scattering, Small Angle”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 901 records · Page 50Linked to original sources

PubMed1998

Morphological observations on liposomes bearing covalently bound protein: studies with freeze-fracture and cryo electron microscopy and small angle X-ray scattering techniques.

The appearance of protein bound to the surface of intact and microfluidized liposomes and its possible influence on their morphology was examined by freeze-fracture electron microscopy, cryo electron microscopy and small angle X-ray scattering (SAXS) techniques. Results obtained by the two microscopy techniques were in agreement with one another in terms of vesicle size and localization of protein (tetanus toxoid or immunoglobulin G) on the surface of vesicles. Surface-bound protein was observed as particles (10-12 nm diameter) by freeze-fracture electron microscopy and was confirmed by immunogold cryo microscopy. SAXS was shown to be a suitable means to further characterize liposomes with, or without bound protein.

Animals↗

PubMed2006

Study of the ordered structures of poly(styrene-b-vinyl4pyridine) in a solution state by using small-angle X-ray scattering and generalized indirect Fourier transform.

The structures of the mesophases and their subunits (micelles) of poly(styrene-b-vinyl4pyridine) (PS-b-P4VP) in a toluene solution were studied by using small-angle X-ray scattering (SAXS), transmission electron microscopy (TEM), and generalized indirect Fourier transform (GIFT) methods. The structures of PS-b-P4VP, such as the individual micelle, the face-centered cubic (fcc) and body-centered cubic (bcc), and the lamellar, were identified. The SAXS from the PS-b-P4VP solution showed a good contrast for the micelle, even in a low concentration of 0.25 wt %. As the concentration increases, the fcc and both fcc and bcc appear for the packing of the micelles of PS(3.3K)-b-P4VP(4.7K) and PS(12K)-b-P4VP(11.8K), respectively. The lamellar structure was also identified, with a further increase in the concentration for PS(3.3K)-b-P4VP(4.7K). These structures were also identified via TEM images.

Journal Article↗

PubMed2002

The solution structure and activation of visual arrestin studied by small-angle X-ray scattering.

Visual arrestin is converted from a 'basal' state to an 'activated' state by interaction with the phosphorylated C-terminus of photoactivated rhodopsin (R*), but the conformational changes in arrestin that lead to activation are unknown. Small-angle X-ray scattering (SAXS) was used to investigate the solution structure of arrestin and characterize changes attendant upon activation. Wild-type arrestin forms dimers with a dissociation constant of 60 micro m. Small conformational changes, consistent with local movements of loops or the mobile N- or C-termini of arrestin, were observed in the presence of a phosphopeptide corresponding to the C-terminus of rhodopsin, and with an R175Q mutant. Because both the phosphopeptide and the R175Q mutation promote binding to unphosphorylated R*, we conclude that arrestin is activated by subtle conformational changes. Most of the arrestin will be in a dimeric state in vivo. Using the arrestin structure as a guide [Hirsch, J.A., Schubert, C., Gurevich, V.V. & Sigler, P.B. (1999) Cell 97, 257-269], we have identified a model for the arrestin dimer that is consistent with our SAXS data. In this model, dimerization is mediated by the C-terminal domain of arrestin, leaving the N-terminal domains free for interaction with phosphorylated R*.

Amino Acid Sequence↗

PubMed2004

Dynamical dimer structure and liquid structure of fatty acids in their binary liquid mixture: dodecanoic and 3-phenylpropionic acids system.

Dimer structure and liquid structure of fatty acids in the binary liquid mixture of dodecanoic (LA) and 3-phenylpropionic acids (PPA) were studied through the measurements of DSC, self-diffusion coefficient (D), density, viscosity, 13C NMR spin-lattice relaxation time, small-angle X-ray scattering (SAXS), and small-angle neutron scattering (SANS). The phase diagram of LA/PPA mixture exhibited a typical eutectic pattern, which means that LA and PPA are completely immiscible in solid phase. In the liquid phase of the LA/PPA mixture, D of LA always differed from that of PPA irrespective of their compositions. This exhibited that, in the liquid phase of the binary mixture of fatty acids giving a complete eutectic in the solid phase, the fatty acid dimers are composed of the same fatty acid species irrespective of their compositions. The liquid structure of the LA/PPA mixture was clarified through the SAXS and also the SANS measurements.

Calorimetry, Differential Scanning↗

PubMed2005

Detailed structure of hairy mixed micelles formed by phosphatidylcholine and PEGylated phospholipids in aqueous media.

Aqueous dispersions of mixed egg yolk phosphatidylcholine (PC) and poly(ethylene glycol) (PEG) modified distearoyl phosphatidylethanolamine (DSPE) were investigated with the purpose of determining shape, size, and conformation of the formed mixed micelles. The samples were prepared at a range of DSPEPEG to PC molar ratios ([DSPEPEG/PC] from 100:0 to 30:70) and with, respectively, DSPEPEG2000 and DSPEPEG5000, where 2000 and 5000 refer to the molar masses of the PEG chains. Particle shape and internal structure were studied using small-angle X-ray scattering (SAXS) and small-angle neutron scattering (SANS). The contrast of the micelles is different for X-rays and neutrons, and by combining SANS and SAXS, complementary information about the micelle structure was obtained. The detailed structure of the micelles was determined in a self-consistent way by fitting a model for the micelles to SANS and SAXS data simultaneously. In general, a model for the micelles with a hydrophobic core, surrounded by a dense hydrophilic layer that is again surrounded by a corona of PEG chains in the form of Gaussian random coils attached to the outer surface, is in good agreement with the scattering data. At high DSPEPEG contents, nearly spherical micelles are formed. As the PC content increases the micelles elongate, and at a DSPEPEG/PC ratio of 30:70, rodlike micelles longer than 1000 angstroms are formed. We demonstrate that by mixing DSPEPEG and PC a considerable latitude in controlling the particle shape is obtained. Our results indicate that the PEG chains in the corona are in a relatively unperturbed Gaussian random coil conformation even though the chains are far above the coil-coil overlap concentration and, therefore, interpenetrating. This observation in combination with the observed growth behavior questions that the "mushroom-brush"transition is the single dominating factor for determining the particle shape as assumed in previous theoretical work (Hristova, K.; Needham, D. Macromolecules 1995, 28, 991-1002).

Hydrophobic and Hydrophilic Interactions↗

PubMed2005

Ternary systems of nonionic surfactant Brij 35, water and various simple alcohols: Structural investigations by small-angle X-ray scattering and dynamic light scattering.

Structural properties of ternary systems composed of nonionic surfactant dodecyl-poly(ethylene oxide-23) ether (C12E23, commercial name: Brij 35), water and various alcohols from ethanol to 1-decanol have been investigated using small-angle X-ray scattering (SAXS) and dynamic light scattering (DLS) techniques. All measurements were performed at the temperature 25 degrees C. SAXS experimental data were put on absolute scale using water as a secondary standard. The data of water-rich mixtures at low to moderate surfactant concentrations were evaluated using the generalized indirect Fourier transformation method (GIFT), which is based on the simultaneous determination of the intra- and inter-particle scattering contributions. In this way, the size and the shape of interacting scattering particles in real space could be deduced. The systems with a relatively low surfactant concentration (5 mass%) were studied most extensively. In these cases, the water-rich regions of the phase diagrams could be investigated into more detail, since in the alcohol-rich regions problems with the GIFT evaluation of the SAXS data were encountered. The presented results demonstrate the level of structural details that can be obtained on the basis of scattering methods and point out the specific stages of data evaluation and interpretation where one must be extremely precautious. As such they reveal the inner structuration of the complex ternary systems of our present interest. In parallel, they also indicate that the longer chain alcohols actually behave as real oil phases in the studied systems, as one might expect, and also confirm the well-known properties of different short to medium chain alcohols that act as co-solvents and/or co-surfactants in microemulsion systems depending on their chain length.

Journal Article↗

PubMed2006

Monitoring intermediate filament assembly by small-angle x-ray scattering reveals the molecular architecture of assembly intermediates.

Intermediate filaments (IFs), along with microtubules, microfilaments, and associated cross-bridging proteins, constitute the cytoskeleton of metazoan cells. While crystallographic data on the dimer representing the elementary IF "building block" have recently become available, little structural detail is known about both the mature IF architecture and its assembly pathway. Here, we have applied solution small-angle x-ray scattering to investigate the in vitro assembly of a 53-kDa human IF protein vimentin at pH 8.4 by systematically varying the ionic strength conditions, and complemented these experiments by electron microscopy and analytical ultracentrifugation. While a vimentin solution in 5 mM Tris.HCl (pH 8.4) contains predominantly tetramers, addition of 20 mM NaCl induces further lateral assembly evidenced by the shift of the sedimentation coefficient and yields a distinct octameric intermediate. Four octamers eventually associate into unit-length filaments (ULFs) that anneal longitudinally. Based on the small-angle x-ray scattering experiments supplemented by crystallographic data and additional structural constraints, 3D molecular models of the vimentin tetramer, octamer, and ULF were constructed. Within each of the three oligomers, the adjacent dimers are aligned exclusively in an approximately half-staggered antiparallel A(11) mode with a distance of 3.2-3.4 nm between their axes. The ULF appears to be a dynamic and a relatively loosely packed structure with a roughly even mass distribution over its cross-section.

Humans↗

PubMed2003

Small angle X-ray scattering study of the yeast prion Ure2p.

The GdmCl-induced equilibrium unfolding and dissociation of the dimeric yeast prion protein Ure2, and its prion domain deletion mutants Delta 15-42Ure2 and 90Ure2, was studied by small angle X-ray scattering (SAXS) using synchrotron radiation and by chemical cross-linking with dithiobis(succinimidyl propionate) (DTSP). The native state is globular and predominantly dimeric prior to the onset of unfolding. R(g) values of 32 and 45A were obtained for the native and 5M GdmCl denatured states of Delta 15-42Ure2, respectively; the corresponding values for 90Ure2 were 2-3A lower. SAXS suggests residual structure in the 4M GdmCl denatured state and chemical cross-linking detects persistence of dimeric structure under these conditions. Hexamers consisting of globular subunits could be detected by SAXS at high protein concentration under partially denaturing conditions. The increased tendency of partially folded states to form small oligomers points to a mechanism for prion formation.

Binding Sites↗

PubMed2001

Collagen orientation and crystallite size in human dentin: a small angle X-ray scattering study.

The mechanical properties of dentin are largely determined by the intertubular dentin matrix, which is a complex composite of type I collagen fibers and a carbonate-rich apatite mineral phase. We performed a small angle X-ray scattering (SAXS) study on fully mineralized human dentin to quantify this fiber/mineral composite architecture from the nanoscopic through continuum length scales. The SAXS results were consistent with nucleation and growth of the apatite phase within periodic gaps in the collagen fibers. These mineralized fibers were perpendicular to the dentinal tubules and parallel with the mineralization growth front. Within the plane of the mineralization front, the mineralized collagen fibers were isotropic near the pulp, but became mildly anisotropic in the mid-dentin. Analysis of the data also indicated that near the pulp the mineral crystallites were approximately needle-like, and progressed to a more plate-like shape near the dentino-enamel junction. The thickness of these crystallites, approximately 5 nm, did not vary significantly with position in the tooth. These results were considered within the context of dentinogenesis and maturation.

Collagen Type I↗

PubMed1996

Small-angle X-ray scattering studies on cellobiose dehydrogenase from Phanerochaete chrysosporium.

Limited proteolysis of cellobiose dehydrogenase (CDH) from the white rot fungus Phanerochaete chrysosporium by papain cleaves the enzyme into two fragments containing flavin (FAD) and heme, respectively. Small-angle X-ray scattering (SAXS) was employed to investigate size and shape of intact CDH and of its fragments in solution. The largest dimension of CDH amounts to about 18 nm, whereas the corresponding quantity of each of the two fragments is only around 9 nm. CDH as well as its fragments appear to be of prolate shape, the cross-section of the FAD fragment (diameter 4.3 to 5.1 nm) being considerably larger than that of the heme fragment (diameter 3.3 nm). These findings suggest a collinear arrangement of the two domains in the CDH particle. Simulations based on the method of finite elements corroborate this structure model and furthermore suggest the existence of a possibly flexible linker between the two domains.

Basidiomycota↗

PubMed2003

Small angle X-ray scattering study of meso-tetrakis (4-sulfonatophenyl) porphyrin in aqueous solution: a self-aggregation model.

The aggregate morphology of meso-tetrakis(4-sulfonatophenyl) porphyrin (TPPS(4)) in aqueous solution is investigated by using small angle x-ray scattering (SAXS) technique. Measurements were performed at pH 4.0 and 9.0 to monitor the pH influence on the structural parameters of the aggregates. Radii of gyration were obtained from distance distribution functions p(r) analysis. The experimental data of TPPS(4) at pH 4.0 showed well-defined oscillations characteristic of large aggregates in contrast to the SAXS curve of 5 mM TPPS(4) at pH 9.0, where both a significant decrease in the intensity and the disappearance of the oscillation peaks suggest the dissociation of the aggregate. A 340-A long "hollow" cylinder with shell thickness of 20 A, compatible to the porphyrin molecule dimension, represents well the scattering curve of the aggregates at pH 4.0. According to the fitting parameters, 26 porphyrin molecules self-associate into a ringlike configuration in the plane of the cylinder cross-section. The total number of porphyrin molecules in the whole aggregate was also estimated as approximately 3000. The model compatible to SAXS data of a hollow cylinder with J-aggregation in the cross-section and H-aggregation (columnar stacking) between the cylinder layers is consistent with optical absorption spectroscopic data both in the literature and obtained in this work.

Computer Simulation↗

PubMed1991

Small-angle X-ray scattering studies of calmodulin mutants with deletions in the linker region of the central helix indicate that the linker region retains a predominantly alpha-helical conformation.

Two mutant forms of calmodulin were examined by small-angle X-ray scattering in solution and compared with the wild-type protein. Each mutant has deletions in the linker region of the central helix: one lacks residues Glu-83 and Glu-84 (Des2) and the other lacks residues Ser-81 through Glu-84 (Des4). The deletions change both the radii of gyration and the maximum dimensions of the molecules. In the presence of Ca2+, the observed radii of gyration are 22.4 A for wild-type bacterially expressed calmodulin, 19.5 A for Des2 calmodulin, and 20.3 A for Des4 calmodulin. A reduction in the radius of gyration by 1-2 A on removal of calcium, previously observed in the native protein, was also found in the wild type and the Des4 mutant; however, no significant size change was observed in the Des2 mutant. The large calcium-dependent conformational change in calmodulin induced by the binding of melittin [Kataoka, M., Head, J.F., Seaton, B.A., & Engelman, D.M. (1989) Proc. Natl. Acad. Sci. U.S.A. 86, 6944-6948] was observed in all the bacterially expressed proteins. Each protein appears to undergo a transition from a dumbbell shape to a more globular conformation on binding melittin in the presence of calcium, although quantitatively the changes in the wild-type and Des4 proteins greatly exceed those in Des2. Modeling shows the central linker region of the molecule. Thus, the structure of the linker region is stable enough to maintain the average orientation and separation of the lobes yet flexible enough to permit the lobes to approach each other upon binding a peptide.

Amino Acid Sequence↗

PubMed1984

A small angle x-ray scattering study of a fragment derived from E. coli 5S RNA.

The structure of a 62 base nuclease resistant fragment of E. coli 5S RNA (bases 1-11, 69-87, 89-120) has been examined by small angle x-ray scattering. The results obtained are indistinguishable from those expected if this oligonucleotide complex were a perfect RNA double helix of about 30 base pairs. These results indicate that this portion of 5S RNA is in a configuration which is approximately double helical, even though proper base pairing is possible over only half its length.

Base Composition↗

PubMed2005

Structure of a full length psychrophilic cellulase from Pseudoalteromonas haloplanktis revealed by X-ray diffraction and small angle X-ray scattering.

Pseudoalteromonas haloplanktis is a psychrophilic Gram-negative bacterium isolated in Antarctica, that lives on organic remains of algae. This bacterium converts the cellulose, highly constitutive of algae, into an immediate nutritive form by biodegrading this biopolymer. To understand the mechanisms of cold adaptation of its enzymatic components, we studied the structural properties of an endoglucanase, Cel5G, by complementary methods, X-ray crystallography and small angle X-ray scattering. Using X-ray crystallography, we determined the structure of the catalytic core module of this family 5 endoglucanase, at 1.4A resolution in its native form and at 1.6A in the cellobiose-bound form. The catalytic module of Cel5G presents the (beta/alpha)(8)-barrel structure typical of clan GH-A of glycoside hydrolase families. The structural comparison of the catalytic core of Cel5G with the mesophilic catalytic core of Cel5A from Erwinia chrysanthemi revealed modifications at the atomic level leading to higher flexibility and thermolability, which might account for the higher activity of Cel5G at low temperatures. Using small angle X-ray scattering we further explored the structure at the entire enzyme level. We analyzed the dimensions, shape, and conformation of Cel5G full length in solution and especially of the linker between the catalytic module and the cellulose-binding module. The results showed that the linker is unstructured, and unusually long and flexible, a peculiarity that distinguishes it from its mesophilic counterpart. Loops formed at the base by disulfide bridges presumably add constraints to stabilize the most extended conformations. These results suggest that the linker plays a major role in cold adaptation of this psychrophilic enzyme, allowing steric optimization of substrate accessibility.

Amino Acid Sequence↗

PubMed1996

Effects of sodium fluoride and alendronate on the bone mineral in minipigs: a small-angle X-ray scattering and backscattered electron imaging study.

Sodium fluoride (NaF), which stimulates bone formation, and bisphosphonates, which reduce bone resorption, are both used in the treatment of osteoporosis, and are binding to bone mineral. In this study, using small-angle X-ray scattering and backscattered electron imaging, we analyzed the bone mineral in the vertebrae of minipigs treated with fluoride, with the bisphosphonate alendronate (ALN), or with vehicle. All specimens were investigated blindly. A slight increase in the average thickness of the mineral crystals as well as changes in the structure of the mineral/collagen composite were found in the case of fluoride-treated animals. No differences were found between ALN-treated animals and controls. The changes produced by fluoride are in the same direction as seen in bones from patients treated with NaF, albeit much smaller. They also correlate quantitatively with the reduction in biomechanical properties of bone in fluoride-treated minipigs found in an earlier study with the same animals. These findings suggest that small changes in the structure of the mineral/collagen composite in bone may considerably affect its biomechanical properties. It also emphasizes the delicate balance between the increase of bone mass and deterioration of bone material properties for the effect of fluoride on the biomechanical properties of bone.

Alendronate↗

PubMed2006

Water soluble quantum dot nanoclusters: energy migration in artifical materials.

Energy migration in self-assembled, water soluble, quantum dot (QD) nanoclusters is reported. These spherical nanoclusters are composed of CdSe QDs bound together by pepsin, a digestive enzyme found in mammals. A structural model for the clusters is suggested, based on scanning transmission electron microscopy, as well as dynamic light scattering and small angle X-ray scattering. Cluster sizes range from 100 to 400 nm in diameter and show a close-packed interior structure. Optical characterization of the absorption and emission spectra of the clusters is reported, finding photoluminescence quantum yields of up to approximately 60% in water for clusters made from core-shell CdSe-ZnS QDs. Clusters prepared from two different size populations of CdSe QD samples (3 and 4 nm in diameter) demonstrate energy migration and trapping. Resonance energy transfer (RET), from small to large dots within the QD-pepsin cluster, is observed by monitoring the quenching of the small donor dot fluorescence along with enhancement of the large acceptor dot fluorescence.

Absorption↗

PubMed2006

Structural transformations during gelatinization of starches in limited water: combined wide- and small-angle X-ray scattering study.

Rice flour (18-25% moisture) and potato starch (20% moisture) were heated with continuous recording of the X-ray scattering during gelatinization. Rice flours displayed A-type crystallinity, which gradually decreased during gelatinization. The development of the characteristic 9 nm small-angle X-ray scattering (SAXS) peak during heating at sub-gelatinization temperatures indicated the gradual evolution into a stacked lamellar system. At higher temperatures, the crystalline and lamellar order was progressively lost. For potato starch (B-type crystallinity), no 9 nm SAXS peak was observed at ambient temperatures. Following the development of lamellar structures at sub-gelatinization temperatures, B-type crystallinity and lamellar order was lost during gelatinization. On cooling of partially gelatinized potato starch, A-type crystallinity steadily increased, but no formation of stacked lamellar structures was observed. Results were interpreted in terms of a high-temperature B- to A-type recrystallization, in which the lateral movement of double helices was accompanied by a shift along their helical axis. The latter is responsible for the inherent frustration of the lamellar stacks.

Chemical Phenomena↗

PubMed2004

Analysis of collagen fibril diameter distribution in connective tissues using small-angle X-ray scattering.

Analysis of the diameters of collagen fibrils provides insight into the structure and physical processes occurring in the tissue. This paper describes a method for analyzing the frequency distribution of the diameters of collagen fibrils from small-angle X-ray scattering (SAXS) patterns. Frequency values of fibril diameters were input into a mathematical model of the form factor to calculate the equatorial intensity which best fits the experimentally derived data from SAXS patterns. A minimization algorithm utilizing simulated annealing (SA) was used in the fitting procedure. The SA algorithm allowed for random sampling of the frequency values, and was run iteratively to build up an optimized frequency distribution of fibril diameters. Results were obtained for collagen samples from sheep spine ligaments. The mean fibril diameter value obtained from this data-fitting method was 73 nm+/-20 nm (S.D.). From scanning transmission electron microscopy, the mean diameter was found to be 69 nm+/-14 nm (S.D.). The good agreement between the two methods demonstrates the reliability of the SAXS method for the tissue examined. The non-destructive nature of this technique, as well as its statistical robusticity and capacity for large sampling, means that this method is both quick and effective.

Algorithms↗