Reinforcing Interlayers of Three-Dimensional-Printed Mortar Using Metal Fiber Insertion

2021 ◽  
Author(s):  
Tomoya Nishiwaki ◽  
Yoshihiro Miyata ◽  
Shoko Furue ◽  
Shiko Fukatsu ◽  
Hideyuki Kajita
Keyword(s):  
Three Dimensional ◽  
Metal Fiber

An Innovative Fabrication Process of Porous Metal Fiber Sintered Felts with Three-Dimensional Reticulated Structure

2010 ◽  
Vol 25 (7) ◽  
pp. 565-571 ◽  
Author(s):  
Yong Tang ◽  
Wei Zhou ◽  
Jianhua Xiang ◽  
Wangyu Liu ◽  
Minqiang Pan
Keyword(s):  
Three Dimensional ◽  
Porous Metal ◽  
Fabrication Process ◽  
Metal Fiber

Manufacturing Process and Geometric Model of Porous Metal Fiber Sintered Felts

2012 ◽  
Vol 499 ◽  
pp. 235-240
Author(s):  
Wei Zhou ◽  
R. Song ◽  
Y. Tang ◽  
Z.P. Wan ◽  
B. Liu
Keyword(s):  
Cell Structure ◽  
Geometric Model ◽  
Three Dimensional ◽  
Porous Metal ◽  
Structure Characteristic ◽  
Test Results ◽  
Dimensional Model ◽  
Metal Fiber ◽  
Three Dimensional Model ◽  
Pore Cell

Using the designed multi-tooth tool, a novel porous metal fiber sintered felt (PMFSF) with three-dimensional reticulated structure has been produced by solid-state sintering of copper fibers. The copper fibers were fabricated using the cutting method. According to the SEM results, it was found that there were two kinds of sintering joints of surface contact and crossing fiber meshing among the fibers in the PMFSF. The coarser sintering joints will help to enhance the mechanical strength of PMFSF. Based on the structure characteristic, a three-dimensional model with the cubic pore cell structure was established to describe the structure of PMFSF. In addition, the effectiveness of geometric model was verified by the test results of specific surface area of PMFSF.

Numerical Simulation of Transport Characteristics of Porous Metal Fiber Sintered Felts Used in Microreactor for Hydrogen Energy

2011 ◽  
Vol 228-229 ◽  
pp. 490-495
Author(s):  
Wei Zhou ◽  
Rong Song ◽  
Zhen Ping Wan ◽  
Yong Tang
Keyword(s):  
Cell Structure ◽  
Catalyst Support ◽  
Three Dimensional ◽  
Porous Metal ◽  
Hydrogen Energy ◽  
Fluid Temperature ◽  
Metal Fiber ◽  
Three Dimensional Model ◽  
Dimensional Network ◽  
Fluent Software

The porous metal fiber sintered felt (PMFSF), a new catalyst support, was successfully used to construct a methanol steam reforming microreactor for hydrogen production. To study the transport characteristics of PMFSFs, a three-dimensional model with the cubic pore cell structure for PMFSFs was established. Using computational fluid dynamics fluent software, the velocity and pressure distribution when the fluid through the PMFSFs was investigated by changing the porosity of PMFSFs and inlet velocity of the fluid. In addition, fluid temperature distribution was analyzed under different inlet velocities by setting the temperature of fluid and wall. The result shows that the PMFSFs greatly enhance the transport characteristics because of its three-dimensional network structure and microchannel structure, it will become an ideal candidate for catalyst support material.

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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