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[Aggregation of tryptophanyl-tRNA synthetase depending on temperature. Study by a low-angle scatter x-ray method].

By means of small angle X-ray scattering, an aggregation of beef pancreas Trp-tRNA synthetase (EC 6.1.1.2) was observed at physiological temperatures. A Trp-tRNA synthetase preparation which is homogeneous after PAGE in beta-ME-SDS was found to be heterogeneous in particle sizes even at low (4-8 degrees C) temperature. At heating up to 30-45 degrees C, the oligomer sizes increased as well as its proportion depending on the incubation time and temperature; very large aggregates were observed 10 times exceeding the sizes of initial particles. Cooling to 20 degrees C caused no disaggregation due to disulphide bond formation between associated subunits of Trp-tRNA synthetase. A hypothesis is proposed that the aggregation of bovine Trp-tRNA synthetase evaluated in vitro and not observed earlier with any aminoacyl-tRNA synthetases of unicellular organisms might serve as one of the mechanisms of its compartmentation in pancreas.

Animals↗
PubMed2006

Organogels with Fe(III) complexes of phosphorus-containing amphiphiles as two-component isothermal gelators.

The properties of thermally reversible organogels in which the gelators consist of a phosphonic acid monoester, phosphonic acid, or phosphoric acid monoester and a ferric salt are probed by IR and NMR spectroscopies, optical microscopy, X-ray diffraction, rheology, and light and small-angle neutron scattering (SANS) techniques. This is one of a small number of two-component molecular gelator systems in which gelation can be induced isothermally. The data indicate that complexation between the phosphonate moieties and Fe(III) is accompanied by their in situ polymerization to form self-assembled fibrillar networks that encapsulate and immobilize macroscopically the organic liquid component. From SANS measurements, the cross-sectional radii of the cyclindrical fibers are ca. 15 A. The efficiencies of the gelators (based on the diversity of the liquids gelated, the minimum concentration of gelator required to make a gel at room temperature, and the temporal and thermal stabilities of the gels) have been determined. With a common ferric salt and liquid component, phosphonic acid monoesters are generally more efficient than phosphinic acids or phosphoric acid esters. Of the phosphonic acid monoesters, monophosphonates are better gelator components than bisphosphonates, and introduction of an omega-hydroxy group on the alkyl chain directly attached to phosphorus reduces significantly gelation ability. Several of the gels are stable for very long periods at room temperature. When heated, they revert to sols over wide temperature ranges. The structures of the gelator complexes and the mechanism of their formation and transformation to gels in selected liquids are examined as well.

Journal Article↗
PubMed2001

Lyotropic phase transitions in phospholipids as evidenced by small-angle synchrotron X-ray scattering.

Hydration is an important factor in regulating the phase behaviour of lipids and besides affects their interactions with other compounds relevant for biological membranes. We present a reliable and fast method to detect and characterise hydration-induced phase transitions in phospholipids by means of small-angle synchrotron X-ray scattering. Films consisting of aggregations of representatives of the two important lipid classes lecithins (DPPC a, POPC and OPPC,a for abbreviations, see below) and cephalins (DPPE and DOPE) were investigated at room temperature in dependence on relative humidity. Qualitative changes in the sets of the diffraction patterns obtained in dynamic hydration/dehydration scans were taken as markers indicating the existence of lyotropic phase transitions. The efficiency of this methodology is demonstrated by illustrating the course of hydration-driven phase transitions between lamellar as well as nonlamellar phases. In detail, this was realised for chain melting in the mixed-chain lipids, POPC and OPPC, and for a novel nonlamellar-phase transition for DOPE between a disordered inverted ribbon phase designated as Palpha and the canonical H(II), phase, respectively.

Macromolecular Substances↗
PubMed1992

Small-angle synchrotron x-ray scattering reveals distinct shape changes of the myosin head during hydrolysis of ATP.

In the energy transduction of muscle contraction, it is important to know the nature and extent of conformational changes of the head portion of the myosin molecules. In the presence of magnesium adenosine triphosphate (MgATP), fairly large conformational changes of the myosin head [subfragment-1 (S1)] in solution were observed by small-angle x-ray scattering with the use of synchrotron radiation as an intense and stable x-ray source. The presence of MgATP reduced the radius of gyration of the molecule by about 3 angstrom units and the maximum chord length by about 10 angstroms, showing that the shape of S1 becomes more compact or round during hydrolysis of MgATP. Comparison with various nucleotide-bound S1 complexes that correspond to the known intermediate states during ATP hydrolysis indicates that the shape of S1 in a key intermediate state, S1-bound adenosine diphosphate (ADP) and phosphate [S1**.ADP.P(i)], differs significantly from the shape in the other intermediate states of the S1 adenosine triphosphatase cycle as well as that of nucleotide-free S1.

Adenosine Triphosphate↗
PubMed1987

Neutron scattering by calf lens cytoplasm. A comparison between two models of cataract.

Small angle neutron scattering (SANS) was used to compare two models of cataracts: the cold cataract induced in the lens nucleus cytoplasm by lowering the temperature and the opacification induced by calcium in the lens cortex cytoplasm. In both cases opacified cytoplasms display additional scattering at low angles as compared to their clear controls. An analysis of this additional scattering provides quantitative information concerning the size distribution, the number and contrast of the scatterers responsible for lens opacification. The scatterers of cold cataract and of calcium--induced opacification not only have, as shown elsewhere, a different composition but are also found to display completely different sizes (in the thousand A range for cold-cataract, in the hundred A range for calcium--induced opacification). These results illustrate the diversity of scatterer types which are able to cause comparable lens opacities.

Animals↗
PubMed2004

Spontaneous vesicle formation and phase behavior in mixtures of an anionic surfactant with imidazoline compounds.

Unexpected colloidal assemblies form in aqueous mixtures of sodium dodecylbenzenesulfonate (SDBS) with the following imidazoline compounds: 2,2'-azobis[2-(2-imidazolin-2-yl)propane] dihydrochloride (V-44, which is a commonly used free-radical initiator), 2,2'-tetramethylenedi-2-imidazoline (TMI), and the main recombination product (RP) from the decomposition of V-44. All of these imidazoline compounds act as hydrotropes. As the molar ratio of imidazoline to SDBS increases, a gradual transition from micelles to vesicles to bilayers to precipitate is observed. V-44 decomposes slowly at 25 degrees C, and the phase diagrams of V-44/SDBS and RP/SDBS are similar. The vesicular region observed in mixtures of TMI/SDBS is larger in composition than that of V-44/SDBS and RP/SDBS mixtures. At equimolar compositions of SDBS and RP, a novel colloidal structure with multiple closely packed bilayers is observed. In these mixtures, small unilamellar vesicles (<80 nm in diameter) form spontaneously, although with time they coexist with a small amount of precipitate and their size increases steadily. The self-assembly of vesicles occurs over a wide range of compositions when the solution pH is lower than the pK(a) of the imidazoline moiety. Quasi-elastic light scattering, cryogenic transmission electron microscopy, nuclear magnetic resonance, and small-angle neutron scattering were used to determine the characteristic length scales and properties of the assemblies.

Journal Article↗
PubMed2005

Oil-in-water microemulsions stabilized by charged diblock copolymers.

We present here oil-in-water microemulsions stabilized by charged diblock copolymers alone, along with their structural characterization by small-angle neutron scattering measurements. They consist of swollen spherical micelles containing small amounts of oil in their core, which is surrounded by a corona of stretched polyelectrolyte chains. Structural changes, including core size variations, are evidenced when using a cosurfactant, or upon addition of salt, through a contraction of the charged corona. Attempts to relate the micellar structure to the individual copolymer characteristics are also presented, and show that the size of the hydrophobic block mainly determines that of the micelles.

Journal Article↗
PubMed1978

Chromatin fiber dimensions and nucleosome orientation: a neutron scattering investigation.

Chromatin fibers were studied in solutions of mM monovalent salt by small angle neutron scattering. The variation of the cross section radius of gyration with H2O/D2O contrast shows that DNA is at much larger average radial distances from the fiber axis than histone. Consequently, the coils of DNA in a core particle must be approximately parallel to the fiber direction. The radii of gyration suggest that the maximum diameter of chromatin and nucleosomes is approximately 14 nm and that the DNA id distributed in two radial layers. The concentration dependence of the scattering maxima near 14 nm spacings furnishes independent support for a 14 nm external diameter and can be interpreted by a double DNA layer configuration.

Animals↗
PubMed2005

The role of counterions on the elasticity of highly charged lamellar phases: a small-angle x-ray and neutron-scattering determination.

The structure and fluctuations of the swollen L(alpha) lamellar phase of highly charged surfactant didodecyldimethylammonium halide fluid bilayers (DDA+X-) are studied using high-resolution small-angle x-ray scattering and medium-resolution, high-contrast small-angle neutron-scattering. The Caille parameter eta, as a function of the swelling (L(alpha) periodicity d), was determined from the full q-range fits of the measured scattering profiles for three different counterions (X- = Cl-, Br-, and NO3-). This parameter quantifies the amplitude of the membrane fluctuations within the Landau-de Gennes smectic-A linear elasticity theory. The different anions used gave strong specific effects at the maximum swelling of the L(alpha) phase, while at lower swellings a two-phase coexistence of swollen and collapsed lamellae (d approximately 30 and approximately 80 angstroms) was observed for bromide and nitrate ions. Over the intermediate dilution range for all three counterions, a single L(alpha) phase can be continuously swollen with pure water which is governed by an equation of state (i.e., osmotic pressure versus period) and thermally excited fluctuation amplitudes that can be well described by the same Poisson-Boltzmann calculation. The membranes were found to be slightly stiffer than predicted by purely electrostatic repulsions, and this is tentatively attributed to an extra bending rigidity contribution from the surfactant chains.

Journal Article↗
PubMed2006

Microfluidic light scattering as a tool to study the structure of aqueous polymer solutions.

A small-angle light scattering (SALS) apparatus, coupled with a specially designed microfluidic device is shown to monitor the formation and subsequent size distribution of giant multilamellar vesicles of a diblock copolymer in aqueous solution. The closed-face design, fabricated between glass slides using a UV-curable optical adhesive, incorporates multiple inlets, a mixing system, and a viewing window to perform on-line SALS. The mixing of each component is tested using polystyrene latex microspheres. Vesicles of the block copolymer, EO6BO11 in aqueous solution are formed on the SALS chip and the pair distance distribution function determined using an inverse Fourier transformation of the scattered intensity to quantify the population and distribution for a range of vesicle sizes. These experiments provide demonstrations of how SALS on a microfluidic device can be used as a rapid screening tool to optimize processing conditions for a range of polymer solutions.

Coloring Agents↗
PubMed2003

Shear-banding and microstructure of colloids in shear flow.

We shall discuss the following phenomena found in various colloidal systems in shear flow. We recently observed shear-banding in suspensions of fd-virus in a cylindrical shear cell. Small angle light scattering experiments revealed that the shear-banding transition is preceded by a relatively fast process (minutes) of nematic-to-paranematic phase separation during which inhomogeneities on the micrometer length scale are formed. After the formation of these inhomogeneities, a slow (hours) appearence of shear-bands is observed, which have a height of a few mm. In the stationary state it is found, by means of polarization microscopy, that inhomogeneities exist within the bands. Small angle, time resolved light scattering experiments on near-critical microstructural order in a mixture of colloidal spheres and free polymer under stationary shear flow are discussed. The unexpected distortion of microstructure in directions perpendicular to the flow direction is quantitatively explained by extending an already existing theory, to include shear-induced short-ranged microstructural distortion. In colloidal systems consisting of "hairy colloids", where a spherical core is decorated with relatively long polymers, shear-induced polymer brush deformation might be important for its structural and rheological behavior. Preliminary neutron scattering and rheology experiments are performed to study polymer brush deformation in (semi-) dilute suspensions.

Journal Article↗
PubMed2001

The overall conformation of conventional kinesins studied by small angle X-ray and neutron scattering.

The quaternary structures of several monomeric and dimeric kinesin constructs from Homo sapiens and Drosophila melanogaster were analyzed using small angle x-ray and neutron scattering. The experimental scattering curves of these proteins were compared with simulated scattering curves calculated from available crystallographic coordinates. These comparisons indicate that the overall conformations of the solution structures of D. melanogaster and H. sapiens kinesin heavy chain dimers are compatible with the crystal structure of dimeric kinesin from Rattus norvegicus. This suggests that the unusual asymmetric conformation of dimeric kinesin in the microtubule-independent ADP state is likely to be a general feature of the kinesin heavy chain subfamily. An intermediate length Drosophila construct (365 residues) is mostly monomeric at low protein concentration whereas at higher concentrations it is dimeric with a tendency to form higher oligomers.

Amino Acid Sequence↗
PubMed2006

Structure of semidilute single-wall carbon nanotube suspensions and gels.

The microscopic network structure of surfactant-stabilized single-wall carbon nanotubes (SWNTs) in water was investigated as a function of SWNT concentration in the semidilute (overlapping) regime using small-angle neutron scattering (SANS). Most of the samples exhibit rigid rod behavior (i.e., Q(-1) intensity variation) at large scattering wavevector, Q, and a crossover to network behavior (i.e., approximately Q(-2) intensity variation) at low Q. The mesh size, xi, of the network was determined from the crossover of rigid rod to network behavior in the SANS intensity profile and was found to decrease with increasing SWNT concentration. When the dispersion quality of these associating rigid rods was degraded, only approximately Q(-2) intensity variation was observed at both high and low Q. Small-angle X-ray scattering measurements of the same stable dispersions were relatively insensitive to network structure because of poor contrast between SWNTs and surfactant.

Gels↗
PubMed1994

Compactness of protein molten globules: temperature-induced structural changes of the apomyoglobin folding intermediate.

Apomyoglobin undergoes a two-step unfolding transition when the pH is lowered from 6 to 2. The partly folded intermediate (I) state at pH 4 and low ionic strength has properties of a molten globule. We have studied structural features of this state, its compactness, content of secondary structure, and specific packing of aromatic side chains, using dynamic light scattering, and small-angle X-ray scattering and far- and near-ultraviolet circular dichroism spectroscopy. Particular attention was paid to temperature-dependent structural changes. The results are discussed with reference to the native-like (N) state and the highly unfolded (U) state. It turned out that the I-state is most compact near 30 degrees C, having a Stokes radius 20% larger and a radius of gyration 30% larger than those of the N-state. Both cooling and heating relative to 30 degrees C led to an expansion of the molecule, but the structural changes at low and high temperatures were of a different kind. At temperatures above 40 degrees C non co-operative melting of structural elements was observed, while the secondary structure was essentially retained on cooling. The results are discussed in context with theoretical predictions of the compactness and the stability of apomyoglobin by Alonso et al. [Alonso, D. O. V., Dill, K. A., and Stigter, D. (1991) Biopolymers 31:1631-1649]. Comparing the I-state of apomyoglobin with the molten globules of alpha-lactalbumin and cytochrome c, we found that the compactness of the molten globule states of the three proteins decreases in the order alpha-lactalbumin > apocytochrome c > apomyoglobin.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1988

Loosening of the phage structure in a low ionic strength environment.

Structural parameters of phage T7 were compared in two frequently used Tris buffers of high and low ionic strength, in order to explain the different biological activity and drug-binding characteristics. Characteristics of the whole phage geometry were obtained by viscosimetry, static and quasi-elastic light-scattering and small-angle X-ray scattering. The latter method revealed dissimilarities in the intraphage DNA compactness, consistent with the findings of the optical absorption melting studies. Alterations in the particle dimensions determined in the same sample by different methods are discussed, and a model is constructed to explain the structural modifications that occur on lowering the ionic strength.

Light↗
PubMed1991

Escherichia coli sigma 70 and NusA proteins. II. Physical properties and self-association states.

In this paper we examine the physical properties and potential for self-association of the Escherichia coli transcription factors, sigma 70 and NusA. We show, by a combination of chemical crosslinking, equilibrium and velocity sedimentation, quasi-elastic light scattering, and small-angle X-ray scattering that NusA exists as a monomer at KCl concentrations between 0.01 and 1.5 M, and that sigma 70 exists as a monomer at KCl concentrations between 0.1 and 1.5 M. The shape and hydration characteristics of each of these monomeric proteins are also examined. The results serve as background for the companion paper in which a thermodynamic analysis is made of the interactions of these transcription factor with E. coli core RNA polymerase in solution and as a component of the functional transcription complex.

Bacterial Proteins↗
PubMed2006

Dissection of a human septin: definition and characterization of distinct domains within human SEPT4.

The septins are a conserved family of guanosine-5'-triphosphate (GTP)-binding proteins. In mammals they are involved in a variety of cellular processes, such as cytokinesis, exocytosis, and vesicle trafficking. Specifically, SEPT4 has also been shown to be expressed in both human colorectal cancer and malignant melanoma, as well as being involved in neurodegenerative disorders. However, many of the details of the modes of action of septins in general remain unclear, and little is known of their detailed molecular architecture. Here, we define explicitly and characterize the domains of human SEPT4. Regions corresponding to the N-terminal, GTPase, and C-terminal domains as well as the latter two together were successfully expressed in Escherichia coli in soluble form and purified by affinity and size-exclusion chromatographies. The purified domains were analyzed by circular dichroism spectroscopy, fluorescence spectroscopy, dynamic light scattering, and small-angle X-ray scattering, as well as with bioinformatics tools. Of the three major domains that comprise SEPT4, the N-terminal domain contains little regular secondary structure and may be intrinsically unstructured. The central GTPase domain is a mixed alpha/beta structure, probably based on an open beta sheet. As defined here, it is catalytically active and forms stable homodimers in vitro. The C-terminal domain also forms homodimers and can be divided into two regions, the second of which is alpha-helical and consistent with a coiled-coil structure. These studies should provide a useful basis for future biophysical studies of SEPT4, including the structural basis for their involvement in diseases such as cancer and neurodegenerative disorders.

Amino Acid Sequence↗