Optimal Displacement Method of Structural Analysis

Author(s):  
A. Kaveh
Author(s):  
Shigetaka HANAI ◽  
Akira KAWASHIMA ◽  
Rintaro ISHIMARU ◽  
Hisashi TANAKA

2011 ◽  
Vol 2011 ◽  
pp. 1-9 ◽  
Author(s):  
Arlindo Pires Lopes ◽  
Adriana Alencar Santos ◽  
Rogério Coelho Lopes

The Moment Distribution Method is a quite powerful hand method of structural analysis, in which the solution is obtained iteratively without even formulating the equations for the unknowns. It was formulated by Professor Cross in an era where computer facilities were not available to solve frame problems that normally require the solution of simultaneous algebraic equations. Its relevance today, in the era of personal computers, is in its insight on how a structure reacts to applied loads by rotating its nodes and thus distributing the loads in the form of member-end moments. Such an insight is the foundation of the modern displacement method. This work has a main objective to present an exact solution for the Moment Distribution Method through a matrix formulation using only one equation. The initial moments at the ends of the members and the distribution and carry-over factors are calculated from the elementary procedures of structural analysis. Four continuous beams are investigated to illustrate the applicability and accuracy of the proposed formulation. The use of a matrix formulation yields excellent results when compared with those in the literature or with a commercial structural program.


1962 ◽  
Vol 66 (617) ◽  
pp. 322-323
Author(s):  
Fernando Venancio Filho

Using the Argyris matrix formulation a concise and definite justification for the correctness of the use of groups of unknowns in the analysis of redundant structures is given. It is shown also that to consider groups of unknowns is equivalent to changing the basic system. These two intimately related concepts are applied to the force as well as to the displacement method.


Author(s):  
W. H. Wu ◽  
R. M. Glaeser

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.


Author(s):  
E. Loren Buhle ◽  
Pamela Rew ◽  
Ueli Aebi

While DNA-dependent RNA polymerase represents one of the key enzymes involved in transcription and ultimately in gene expression in procaryotic and eucaryotic cells, little progress has been made towards elucidation of its 3-D structure at the molecular level over the past few years. This is mainly because to date no 3-D crystals suitable for X-ray diffraction analysis have been obtained with this rather large (MW ~500 kd) multi-subunit (α2ββ'ζ). As an alternative, we have been trying to form ordered arrays of RNA polymerase from E. coli suitable for structural analysis in the electron microscope combined with image processing. Here we report about helical polymers induced from holoenzyme (α2ββ'ζ) at low ionic strength with 5-7 mM MnCl2 (see Fig. 1a). The presence of the ζ-subunit (MW 86 kd) is required to form these polymers, since the core enzyme (α2ββ') does fail to assemble into such structures under these conditions.


Author(s):  
Paul DeCosta ◽  
Kyugon Cho ◽  
Stephen Shemlon ◽  
Heesung Jun ◽  
Stanley M. Dunn

Introduction: The analysis and interpretation of electron micrographs of cells and tissues, often requires the accurate extraction of structural networks, which either provide immediate 2D or 3D information, or from which the desired information can be inferred. The images of these structures contain lines and/or curves whose orientation, lengths, and intersections characterize the overall network.Some examples exist of studies that have been done in the analysis of networks of natural structures. In, Sebok and Roemer determine the complexity of nerve structures in an EM formed slide. Here the number of nodes that exist in the image describes how dense nerve fibers are in a particular region of the skin. Hildith proposes a network structural analysis algorithm for the automatic classification of chromosome spreads (type, relative size and orientation).


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