Three dimensional morphology of the dumbbell nebula and the ring nebula

2009 ◽  
Author(s):  
Sze-ning Chong
2007 ◽  
Vol 134 (4) ◽  
pp. 1679-1692 ◽  
Author(s):  
C. R. O'Dell ◽  
F. Sabbadin ◽  
W. J. Henney

1988 ◽  
Vol 130 ◽  
pp. 598-598
Author(s):  
Avishai Dekel ◽  
Erez Braun

A noticeable fact about the giant luminous arcs, which have been detected in a few high-redshift clusters of galaxies (see contributions by Petrosian and by Mellier in this volume), is that they seem to be segments of almost perfectly circular rings – in one case spanning about one third of a circle. If this is a characteristic property of these arcs, they cannot be segments of randomly-oriented three-dimensional rings, which, when viewed from a random direction, should look acircular in most cases. Perhaps the most generic source for a circular ring is a limb-brightened luminous shell – as in planetary nebulae and supernova remnants. Such shells can naturally arise, for example, from explosion-generated shocks which cooled and fragmented into stars. If the sources are shells, and the arcs are either resolved or their thickness is determined by the seeing conditions (and by the CCD pixle size), there is a very general upper-limit on the possible surface-brightness contrast between the arcs and the regions encompassed by them. For the detected arcs, without any special finetuning, this limit is ≃ 3. It might become twice as big if the shell is transparent and the interior is opaque. This limit could exclude the shell model if the preliminary claims for a detected contrast greater than 10 are confirmed. It is interesting to note that the famous ring nebula presents a similar problem. We checked several mechanisms, such as stimulated radiation, which could, in principle, enhance the observed contrast while retaining the spherical symmetry; if such a mechanism is responsible for the enhanced contrast, it should show clear imprints on the spectrum. The figure shows the surface-brightess profile for a shell of thickness d.


2016 ◽  
Vol 12 (S323) ◽  
pp. 345-347
Author(s):  
Marcelo L. Leal-Ferreira ◽  
Isabel Aleman ◽  
Andrea Gaughan ◽  
Djazia Ladjal ◽  
Toshiya Ueta ◽  
...  

AbstractWe observed the Planetary Nebula NGC 6720 with the Gemini Telescope and the Gemini Multi-Object Spectrographs. We obtained spatial maps of 36 emission-lines in the wavelength range between 3600 Å and 9400 Å. We derived maps of c(Hβ), electronic densities, electronic temperatures, ionic and elemental abundances, and Ionization Correction Factors (ICFs) in the source and investigated the mass-loss history of the progenitor. The elemental abundance results indicate the need for ICFs based on three-dimensional photoionization models.


1966 ◽  
Vol 25 ◽  
pp. 227-229 ◽  
Author(s):  
D. Brouwer

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.


Author(s):  
M. Boublik ◽  
W. Hellmann ◽  
F. Jenkins

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.


Author(s):  
P.L. Moore

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.


Author(s):  
G. Stöffler ◽  
R.W. Bald ◽  
J. Dieckhoff ◽  
H. Eckhard ◽  
R. Lührmann ◽  
...  

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).


Author(s):  
James A. Lake

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.


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