Evaluation of the Cognitive Process during Mental Imaging of Two- or Three-Dimensional Figures

2009 ◽  
Author(s):  
Koji Kashihara
Keyword(s):  
Cognitive Process ◽  
Three Dimensional ◽  
Mental Imaging

scholarly journals Simulación de Mecanismos

2019 ◽  
pp. 20-27
Author(s):  
Homero Jiménez-Rabiela ◽  
Benjamín Vázquez-González ◽  
José Luis Ramírez-Cruz ◽  
Pedro García-Segura
Keyword(s):  
Quantitative Analysis ◽  
Cognitive Process ◽  
Degrees Of Freedom ◽  
Three Dimensional ◽  
Qualitative And Quantitative Analysis ◽  
Mechanical Advantage ◽  
Qualitative And Quantitative

Objectives: In this work we show different simulated mechanisms virtually, their objective is to facilitate the qualitative and quantitative analysis of their kinematics; allowing to determine degrees of freedom, relation of times, mechanical advantage, mobility, positions, speeds and accelerations. Such an objective is achieved by simulating them for different positions using discretization and variable timing. Methodology: It consists of files of mechanisms with the corresponding files of links and electronic spreadsheets. The student must modify the dimensional, geometric and kinematic restrictions; remove them and install new ones; to observe the behavior of the mechanism as a system or of the links as integral parts. Contribution: Simplify the cognitive process of the kinematics of the mechanisms. It facilitates the understanding of the Euler and the Lagrange approaches. It allows to understand and evaluate the positions, speeds and accelerations; absolute, relative and apparent. The files of mechanisms and links are virtual, three-dimensional and allow their animation. Electronic spreadsheets control the restrictions of both the mechanisms and their links.

Technology Study on the Different Cognitive Process of Stereopsis between Crossed and Uncrossed Fine Disparity

2014 ◽  
Vol 886 ◽  
pp. 374-377
Author(s):  
Yan Wu ◽  
Qi Li
Keyword(s):  
Visual System ◽  
Human Visual System ◽  
Cognitive Process ◽  
Three Dimensional ◽  
Reaction Times ◽  
Visual Fatigue ◽  
Technology Study ◽  
Random Dot Stereograms ◽  
Display Technology ◽  
Made In

Considerable improvements in display technology were made in stereoscopic imaging and image quality rose with technical progress. But there was not enough effort on reducing visual fatigue. The study was to investigate one of the ways to reduce visual fatigue caused by three-dimensional images. Static random-dot stereograms (RDS) were used as stimuli. The performance of every subject was recorded with disparate disparities of 3.27', 6.54', 8.18', 11.45', 14.72', 17.99', 21.26', and 24.53'. Results showed that reaction times were always longer in the uncrossed disparities relative to the crossed disparities. For crossed disparities, human visual system was the most sensitive to the images with disparity of 6.54'. As to uncrossed disparities, human visual system was the most sensitive to the images with disparity of 8.18'.

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).

Sign in / Sign up

Export Citation Format

Share Document