• Journal of the Computational Structural Engineering Institute of Korea
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• v.36 no.4
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• pp.213-220
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• 2023

This paper presents a model simulating the folding process and collision dynamics of "ddakji", a traditional Korean game played using paper tiles (which are also referred to as ddakji). The model uses two A4 sheets as the base materials for ddakji. The folding process involves a series of boundary conditions that transform the wing part of the paper structure into a twisted configuration. A rigid plate boundary condition is also adopted for squeezing, establishing the shape and stress state of the game-ready ddakji through dynamic relaxation analysis. The gaming process analysis involves a forced displacement of the striking ddakji to a predetermined collision position. Collision analysis then follows at a given speed, with the objective of overturning the struck ddakji--a winning condition. A genetic algorithm-based optimization analysis identifies the optimal collision conditions that result in the overturning of the struck ddakji. For efficiency, the collision analysis is divided into two stages, with the second stage carried out only if the first stage predicts a possible overturn. The fitness function for the genetic algorithm during the first stage is the direction cosine of the struck ddakji, whereas in the second stage, it is the inverse of the speed, thus targeting the lowest overall collision speed. Consequently, this analysis provides optimal collision conditions for various compression thicknesses.

• Journal of Microbiology and Biotechnology
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• v.26 no.7
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• pp.1163-1172
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• 2016

The Ω-loop is a nonregular and flexible structure that plays an important role in molecular recognition, protein folding, and thermostability. In the present study, molecular dynamics simulation was carried out to assess the molecular stability and flexibility profile of the porcine trypsin structures. Two Ω-Loops (fragment 57-67 and fragment 78-91) were confirmed to represent the flexible region. Subsequently, glycosylation site-directed mutations (A73S, N84S, and R104S) were introduced within the Ω-loop region and its wing chain based on its potential N-glycosylation sites (Asn-Xaa-Ser/Thr consensus sequences) and structure information to improve the thermostability of trypsin. The result demonstrated that the half-life of the N84S mutant at 50℃ increased by 177.89 min when compared with that of the wild-type enzyme. Furthermore, the significant increase in the thermal stability of the N84S mutant has also been proven by an increase in the T_m values determined by circular dichroism. Additionally, the optimum temperatures of the wild-type enzyme and the N84S mutant were 75℃ and 80℃, respectively. In conclusion, we obtained the thermostability-improved enzyme N84S mutant, and the strategy used to design this mutant based on its structural information and N-linked glycosylation modification could be applied to engineer other enzymes to meet the needs of the biotechnological industry.