The domain superposition technique for solving three-dimensional piecewise homogeneous laplace problems

2020 ◽  
Vol 199 ◽  
pp. 85-94 ◽  
Author(s):  
J.P. Barbosa ◽  
L.O.C. Lara ◽  
C.F. Loeffler
Keyword(s):  
Three Dimensional ◽  
Superposition Technique

Numerical Simulation of Fluid Flow and Mixing Dynamics inside Planetary Roller Extruders

2021 ◽  
Vol 36 (5) ◽  
pp. 508-518
Author(s):  
J. Winck ◽  
S. Frerich
Keyword(s):  
Fluid Flow ◽  
Extensional Flow ◽  
Three Dimensional ◽  
Numerical Approach ◽  
High Rate ◽  
Mixing Dynamics ◽  
Residence Time Distributions ◽  
Process Behavior ◽  
Superposition Technique ◽  
Dispersive Mixing

Abstract In this contribution, the fluid flow and mixing dynamics inside planetary roller extruders are simulated using the finite element method (FEM) and the mesh superposition technique (MST). Three-dimensional configurations with planetary spindles of varying number and geometry of planetary spindles were created to analyse the influence of the spindle configuration and the rotational speed on the process behavior. Therefore, pressure gradients, flow velocities and directions, shear rates, the mixing index and residence time distributions were evaluated. The distributive and dispersive mixing efficiencies varied depending on the planetary spindle configuration, and these configurations thus suit different processing tasks. In comparison to the standard planetary spindles, the TT3 spindles, with their incomplete toothing, and the knob spindles, with their double transversal helical toothing, showed intense axial and radial mixing. In general, the mixing performance of the planetary roller extruder is explained by a high rate of extensional flow and frequent changes in flow type. The reported numerical approach allows, for the first time, a comprehensive observation of the process behavior of planetary roller extruders.

scholarly journals A new model for the Milky Way bar

2012 ◽  
Vol 10 (H16) ◽  
pp. 350-350
Author(s):  
Yougang Wang ◽  
Hongsheng Zhao ◽  
Shude Mao ◽  
R. M. Rich
Keyword(s):  
Velocity Dispersion ◽  
Three Dimensional ◽  
Longitudinal Direction ◽  
Proper Motions ◽  
Density Distributions ◽  
Disk Mass ◽  
Dispersion Data ◽  
Pattern Speed ◽  
Superposition Technique ◽  
Best Fit

AbstractWe use Schwarzschild's orbit-superposition technique to construct self-consistent models of the Galactic bar. Using χ2 minimisation, we find that the best-fit Galactic bar model has a pattern speed Ωp=60 km s−1 kpc−1, disk mass Md=1.0×1011M⊙ and bar angle θbar=20° for an adopted bar mass Mbar=2×1010M⊙. The model can reproduce not only the three-dimensional and projected density distributions but also velocity and velocity dispersion data from the BRAVA survey. We also predict the proper motions in the range l=[−12°,12°], b=[−10°,10°], which appear to be higher than observations in the longitudinal direction. The model is stable within a timescale of 0.5 Gyr, but appears to deviate from steady-state on longer timescales. Our model can be further tested by future observations such as those from GAIA.

The orbit of Pluto over a long interval of time

1966 ◽  
Vol 25 ◽  
pp. 227-229 ◽  
Author(s):  
D. Brouwer
Keyword(s):  
Periodic Orbit ◽  
Numerical Integration ◽  
Restricted Problem ◽  
Three Dimensional ◽  
The Third ◽  
Circular Restricted Problem ◽  
Resonance Relation

The paper presents a summary of the results obtained by C. J. Cohen and E. C. Hubbard, who established by numerical integration that a resonance relation exists between the orbits of Neptune and Pluto. The problem may be explored further by approximating the motion of Pluto by that of a particle with negligible mass in the three-dimensional (circular) restricted problem. The mass of Pluto and the eccentricity of Neptune's orbit are ignored in this approximation. Significant features of the problem appear to be the presence of two critical arguments and the possibility that the orbit may be related to a periodic orbit of the third kind.

Conformation of Ribosomes from Escherichia Coli

1974 ◽  
Vol 32 ◽  
pp. 210-211
Author(s):  
M. Boublik ◽  
W. Hellmann ◽  
F. Jenkins
Keyword(s):  
Binding Sites ◽  
Ribosomal Proteins ◽  
Fluorescent Dyes ◽  
Protein Biosynthesis ◽  
Three Dimensional ◽  
Spatial Arrangement ◽  
Dimensional Structure ◽  
Complete Understanding ◽  
And Function

The present knowledge of the three-dimensional structure of ribosomes is far too limited to enable a complete understanding of the various roles which ribosomes play in protein biosynthesis. The spatial arrangement of proteins and ribonuclec acids in ribosomes can be analysed in many ways. Determination of binding sites for individual proteins on ribonuclec acid and locations of the mutual positions of proteins on the ribosome using labeling with fluorescent dyes, cross-linking reagents, neutron-diffraction or antibodies against ribosomal proteins seem to be most successful approaches. Structure and function of ribosomes can be correlated be depleting the complete ribosomes of some proteins to the functionally inactive core and by subsequent partial reconstitution in order to regain active ribosomal particles.

Ultrastructural Investigations of the Contractile Filaments of Amoebae

1974 ◽  
Vol 32 ◽  
pp. 188-189
Author(s):  
P.L. Moore
Keyword(s):  
Cytoplasmic Streaming ◽  
Three Dimensional ◽  
Freeze Fracture ◽  
Amoeboid Movement ◽  
Different Types ◽  
Chemical Conditions ◽  
Complete Interpretation

Previous freeze fracture results on the intact giant, amoeba Chaos carolinensis indicated the presence of a fibrillar arrangement of filaments within the cytoplasm. A complete interpretation of the three dimensional ultrastructure of these structures, and their possible role in amoeboid movement was not possible, since comparable results could not be obtained with conventional fixation of intact amoebae. Progress in interpreting the freeze fracture images of amoebae required a more thorough understanding of the different types of filaments present in amoebae, and of the ways in which they could be organized while remaining functional.The recent development of a calcium sensitive, demembranated, amoeboid model of Chaos carolinensis has made it possible to achieve a better understanding of such functional arrangements of amoeboid filaments. In these models the motility of demembranated cytoplasm can be controlled in vitro, and the chemical conditions necessary for contractility, and cytoplasmic streaming can be investigated. It is clear from these studies that “fibrils” exist in amoeboid models, and that they are capable of contracting along their length under conditions similar to those which cause contraction in vertebrate muscles.

Structural organization of escherichia coli ribosomes as determined by immuno electron microscopy

1978 ◽  
Vol 36 (2) ◽  
pp. 166-167 ◽  
Author(s):  
G. Stöffler ◽  
R.W. Bald ◽  
J. Dieckhoff ◽  
H. Eckhard ◽  
R. Lührmann ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Escherichia Coli ◽  
Ribosomal Proteins ◽  
Structural Organization ◽  
Three Dimensional ◽  
Ribosomal Subunit ◽  
Spatial Arrangement ◽  
Small Subunit ◽  
Antibody Binding ◽  
Immuno Electron Microscopy

A central step towards an understanding of the structure and function of the Escherichia coli ribosome, a large multicomponent assembly, is the elucidation of the spatial arrangement of its 54 proteins and its three rRNA molecules. The structural organization of ribosomal components has been investigated by a number of experimental approaches. Specific antibodies directed against each of the 54 ribosomal proteins of Escherichia coli have been performed to examine antibody-subunit complexes by electron microscopy. The position of the bound antibody, specific for a particular protein, can be determined; it indicates the location of the corresponding protein on the ribosomal surface.The three-dimensional distribution of each of the 21 small subunit proteins on the ribosomal surface has been determined by immuno electron microscopy: the 21 proteins have been found exposed with altogether 43 antibody binding sites. Each one of 12 proteins showed antibody binding at remote positions on the subunit surface, indicating highly extended conformations of the proteins concerned within the 30S ribosomal subunit; the remaining proteins are, however, not necessarily globular in shape (Fig. 1).

Ribosome Structural Organization

1974 ◽  
Vol 32 ◽  
pp. 332-333
Author(s):  
James A. Lake
Keyword(s):  
Ribosomal Proteins ◽  
Structural Organization ◽  
Three Dimensional ◽  
Small Subunit ◽  
Structural Studies ◽  
X Ray Diffraction ◽  
Specific Antibodies ◽  
X Ray ◽  
E Coli ◽  
Complete Sequences

The understanding of ribosome structure has advanced considerably in the last several years. Biochemists have characterized the constituent proteins and rRNA's of ribosomes. Complete sequences have been determined for some ribosomal proteins and specific antibodies have been prepared against all E. coli small subunit proteins. In addition, a number of naturally occuring systems of three dimensional ribosome crystals which are suitable for structural studies have been observed in eukaryotes. Although the crystals are, in general, too small for X-ray diffraction, their size is ideal for electron microscopy.

Sign in / Sign up

Export Citation Format

Share Document