A generalized hybrid transfinite element computational approach for nonlinear/linear unified thermal-structural analysis

Structural analysis of variable topology mechanisms (VTMs) is the leading task when studying the topological variability of mechanisms. Of several major concerns, structure decomposition and homomorphism identification are two dominating issues for the structural analysis of VTMs. This paper presents a systematic computational approach for the structure decomposition and homomorphism identification of planar VTMs. Along with the proposed method, a constraint matrix representation, that records the potential motion constraints and the topological structures of a VTM, is introduced for serving as the basis of the approach. In addition, a new index, namely, degrees of homomorphism (DOHs), is suggested for quantifying the topological similarity among VTMs. For illustration, an automatic steel clamping and sawing mechanism and a group of mechanisms with similar topologies are adopted, from which their structure decomposition and homomorphism identification are carried out. As shown, the method is both symbolically readable and computationally considerable. The result is helpful for the automated structural analysis and synthesis of variable topology mechanisms.

Download Full-text

Structural Analysis of G1691S Variant in the Human Filamin B Gene Responsible for Larsen Syndrome: A Comparative Computational Approach

Journal of Cellular Biochemistry ◽

10.1002/jcb.25920 ◽

2017 ◽

Vol 118 (7) ◽

pp. 1900-1910 ◽

Cited By ~ 27

Author(s):

Sneha P ◽

Kumar Thirumal D ◽

Himani Tanwar ◽

Siva R ◽

George Priya Doss C ◽

...

Keyword(s):

Structural Analysis ◽

Computational Approach ◽

Larsen Syndrome ◽

Filamin B

Download Full-text

The structural analysis of MARK4 and the exploration of specific inhibitors for the MARK family: a computational approach to obstruct the role of MARK4 in prostate cancer progression

Molecular BioSystems ◽

10.1039/c3mb70591a ◽

2014 ◽

Vol 10 (7) ◽

pp. 1845-1868 ◽

Cited By ~ 21

Author(s):

Pranitha Jenardhanan ◽

Jayakanthan Mannu ◽

Premendu P. Mathur

Keyword(s):

Prostate Cancer ◽

Structural Analysis ◽

Cancer Progression ◽

Computational Approach ◽

Prostate Cancer Progression ◽

Inactive State ◽

Specific Inhibitors

The binding of identified ATP competitors specific to MARK4, characterized by a unique DFG Asp-in/αC helix-out inactive state, hampers the progression of prostate cancer.

Download Full-text

Application of Modified Bloch Waves to Image Analysis of Extended Linear Defects

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s042482010005202x ◽

1974 ◽

Vol 32 ◽

pp. 402-403

Author(s):

S. Nakahara ◽

D. M. Maher

Keyword(s):

Image Analysis ◽

Computational Approach ◽

Dislocation Loops ◽

Plane Wave Expansion ◽

Dynamical Equations ◽

Bloch Waves ◽

Linear Defects ◽

Imperfect Crystal ◽

Localized Defects ◽

Defective Crystals

Since Head first demonstrated the advantages of computer displayed theoretical intensities from defective crystals, computer display techniques have become important in image analysis. However the computational methods employed resort largely to numerical integration of the dynamical equations of electron diffraction. As a consequence, the interpretation of the results in terms of the defect displacement field and diffracting variables is difficult to follow in detail. In contrast to this type of computational approach which is based on a plane-wave expansion of the excited waves within the crystal (i.e. Darwin representation ), Wilkens assumed scattering of modified Bloch waves by an imperfect crystal. For localized defects, the wave amplitudes can be described analytically and this formulation has been used successfully to predict the black-white symmetry of images arising from small dislocation loops.

Download Full-text

Structural analysis of the surface-layer protein of spirillum serpens by high-resolution electron microscopy

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100077268 ◽

1983 ◽

Vol 41 ◽

pp. 738-739

Author(s):

W. H. Wu ◽

R. M. Glaeser

Keyword(s):

Electron Microscopy ◽

Surface Layer ◽

Structural Analysis ◽

High Resolution ◽

Low Dose ◽

High Resolution Electron Microscopy ◽

Optical Diffraction ◽

Surface Layer Protein ◽

Morphological Unit ◽

Resolution Electron

Spirillum serpens possesses a surface layer protein which exhibits a regular hexagonal packing of the morphological subunits. A morphological model of the structure of the protein has been proposed at a resolution of about 25 Å, in which the morphological unit might be described as having the appearance of a flared-out, hollow cylinder with six ÅspokesÅ at the flared end. In order to understand the detailed association of the macromolecules, it is necessary to do a high resolution structural analysis. Large, single layered arrays of the surface layer protein have been obtained for this purpose by means of extensive heating in high CaCl2, a procedure derived from that of Buckmire and Murray. Low dose, low temperature electron microscopy has been applied to the large arrays.As a first step, the samples were negatively stained with neutralized phosphotungstic acid, and the specimens were imaged at 40,000 magnification by use of a high resolution cold stage on a JE0L 100B. Low dose images were recorded with exposures of 7-9 electrons/Å2. The micrographs obtained (Fig. 1) were examined by use of optical diffraction (Fig. 2) to tell what areas were especially well ordered.

Download Full-text