Chapter

Understanding Cross-Sections

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Abstract

This chapter provides the basis for the study and understanding of the structural cross-sections. The anatomy and hierarchy of the cross-section shapes, types, and the materials they are made up is extensively covered. Several methods for defining the cross-sections, including parametric and general procedures, are discussed. The main focus of the chapter is to provide closed-form solutions for computing the geometric properties of various section shapes. It also discusses general polygon and mesh-based procedures for solution of composite and complex sections. In addition to the formulae to compute the properties, a discussion on the significance of various properties helps us to improve the cross-sectional behavior of computer-based methods, and several solved examples are included followed by problems for readers to try and explore. The chapter makes use of extensive illustrations and diagrams.

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... Rg is the RMS distance of all electrons from their center of gravity [13], used to measure of the elastic stability of a cross-section [14]. The Rg values of WT and mutations throughout the simulation time period were examined simultaneously, and variations in folding state were observed. ...
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Studying the structure of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike (S) protein is important to understand the infection process. The S protein is necessary in completing the virus life cycle and is responsible for the appearance of new variants and drug and vaccine resistance. Understanding the structure and dynamics of biological macromolecules is essential for understanding how they function. In this work, we investigated the effects of mutations on S protein stability and solubility through molecular dynamic (MD) simulation in a 100 ns (ns) period. We screened four variants in addition to the wild type (WT). Results show that changes on MD simulation parameters of S protein indicate fluctuations and changes in the conformation, especially in the area between 300 and 600 amino acids (aa). This provides us an image of how the virus protein can reshape itself to adapt to any changes that occur in human angiotensin-converting enzyme 2 or drugs that can target the protein region. Our results also show that the Brazil variant has high fluctuations and unstable folding at some stages compared with other variants.
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