scholarly journals Magnetic Investigation of an Atypical Three-Dimensional Bimetallic Oxalate-Based Magnet

2019 ◽  
Vol 124 (1) ◽  
pp. 952-957 ◽  
Author(s):  
Virginie Simonet ◽  
Françoise Damay ◽  
Sylvie Ferlay ◽  
Andrew Cea ◽  
Catalin Maxim ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Magnetic Investigation

A three-dimensional cyanide-bridged heterometallic coordination polymer: poly[[diacetonitrilediaqua[μ2-3,6-bis(pyridin-2-yl)-1,2,4,5-tetrazine-κ4N1,N6:N3,N4]tetra-μ-cyanido-tetracyanidodimanganese(II)molybdate(IV)] dihydrate]

2014 ◽  
Vol 70 (11) ◽  
pp. 1029-1032 ◽  
Author(s):  
Xiao-Juan Xu
Keyword(s):  
Magnetic Properties ◽  
Ir Spectroscopy ◽  
Coordination Polymer ◽  
Elemental Analysis ◽  
Room Temperature ◽  
Three Dimensional ◽  
Antiferromagnetic Coupling ◽  
X Ray Diffraction ◽  
X Ray ◽  
Magnetic Investigation

A metal coordination polymer, {[Mn2Mo(CN)8(C12H8N6)(CH3CN)2(H2O)2]·2H2O}n, has been synthesized by the reaction of Mn(ClO4)2·6H2O with 3,6-bis(pyridin-2-yl)-1,2,4,5-tetrazine (bptz) and (Bu3N)3[Mo(CN)8] at room temperature. The polymer was characterized by IR spectroscopy, elemental analysis and X-ray diffraction, and the magnetic properties were also investigated. The X-ray diffraction analysis reveals that the compound is a new three-dimensional coordination polymer with a PtS-type network. Magnetic investigation shows antiferromagnetic coupling between adjacent Mn2+cations.

A novel tetrazolate- and cyanide-bridged three-dimensional heterometallic coordination polymer: crystal structure, thermal stability and magnetic properties

2017 ◽  
Vol 73 (11) ◽  
pp. 968-974 ◽  
Author(s):  
Ying-Lian Qin ◽  
Jian-Fang Qin ◽  
Hong Sun
Keyword(s):  
Crystal Structure ◽  
Magnetic Measurements ◽  
Three Dimensional ◽  
Crystal Structure Analysis ◽  
Antiferromagnetic Coupling ◽  
Solvothermal Reaction ◽  
X Ray ◽  
Magnetic Investigation ◽  
Ft Ir ◽  
Scanning Electron

By using environmentally friendly K3[Co(CN)6] as a cyanide source, the solvothermal reaction of CuCl2 and tetrazole (Htta) led to a novel tetrazolate- and cyanide-bridged three-dimensional heterometallic CuII–CoIII complex, namely poly[[hexa-μ2-cyanido-κ12 C:N-pentakis(μ3-tetrazolato-κ3 N 1:N 2:N 4)cobalt(III)tetracopper(II)] monohydrate], {[CoIIICuII 4(CHN4)5(CN)6]·H2O} n , (I). The crystal structure analysis reveals that it is the first example of a (6,8,8)-connected three-dimensional framework with a unique topology, constructed from anionic [Co(CN)6]3− and cationic [(Cu1)2(tta)2]2+ and [(Cu2Cu3)(tta)3]+ units through μ2-cyanide and μ3-tetrazolate linkers. The compound was further characterized by thermal analysis, vibrational spectroscopy (FT–IR), scanning electron microscopy/energy-dispersive X-ray spectroscopy (SEM–EDS) and magnetic measurements. The magnetic investigation indicates that the complex exhibits antiferromagnetic coupling between adjacent CuII cations.

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).

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