• Journal of Life Science
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• v.8 no.2
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• pp.223-233
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• 1998

Discovery of molecular chaperone has stimulate cell biologists and thus made it possible to re-examine the processes whereby proteins achieve and maintain their functional conformations within living cells. the term ‘Molecular chaperone’ was first coined to describe one particular protein involved in the assembly of nucleosomes, but the term has now been extended to describe the function of a wide variety of proteins that assist protein transport across membranes, folding of nascent polypeptide, the assembly and disassembly of oligomeric structures, and the recovery or removal of proteins damaged by various environmental stresses including heat shock. Progress of molecular chaperone research is still limited by the lack of 3-dimensional structural information and detailed interacts with taget proteins in the cell. However, several laboratories around the world are attempting to extend our knowledge on the functions of molecular chaperone, and such efforts seem justified to finally provide the answers to the most burning questions shortly.

• BMB Reports
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• v.41 no.11
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• pp.820-825
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• 2008

Bacillus thuringiensis Cyt2Aa toxin is a mosquito-larvicidal and cytolytic $\delta$-endotoxin, which is synthesized as a protoxin and forms crystalline inclusions within the cell. These inclusions are solubilized under alkaline conditions and are activated by proteases within the larval gut. In order to assess the functions of the N-and C-terminal regions of the protoxin, several N- and C-terminal truncated forms of Cyt2Aa were constructed. It was determined that amino acid removal at the N-terminal, which disrupts the $\beta$1 structure, might critically influence toxin production and inclusion formation. The deletion of 22 amino acids from the C-terminus reduced the production and solubility of the toxin. However, the removal of more than 22 amino acids from the C-terminus or the addition of a bulky group to this region could result in the inability of the protein to adopt the proper folding. These findings directly demonstrated the critical roles of N- and C-terminal amino acids on the production and folding of the B. thuringiensis cytolytic $\delta$-endotoxin.

• Atmosphere
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• v.23 no.3
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• pp.331-346
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• 2013

A case study of mesoscale snowfall with polar low signature during 25~26 December 2010 in South Korea is presented. The data used for analysis include surface and upper level weather charts, rain gauge, sea surface temperature, satellite imagery, sounding, and global $1^{\circ}{\times}1^{\circ}$ reanalysis data. The system initiated with a surface trough near the bay of Bohai but quickly intensified to become a polar low within 12 hours. The polar low moved southeastward bringing snowfall to southwestern Korea. There was strong instability layer beneath 800 hPa but baroclinicty was weak and disappeared as the low progressed onto land. Shortwave at 500 hPa and the surface trough became in-phase which hindered the development of the polar low while it approached Korea. However, there were strong tropopause folding (~500 hPa) and high potential vorticity (PV), which allowed the system to maintain its structure and dump 20.3 cm of snow in Jeonju. Synoptic, thermodynamic, dynamic, and moisture analyses reveal that polar low developed in an area of baroclinicity with strong conditional instability and warm air advection at the lower levels. Further, the development of a surface trough to polar low was aided by tropopause folding with PV advection in the upper level, shortwave trough at 500 hPa, and moisture advection with low-level jet (LLJ) of 15 m $s^{-1}$ or more at 850 hPa. Maximum snowfall was concentrated in this region with convection being sustained by latent heat release.

• BMB Reports
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• v.40 no.4
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• pp.453-458
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• 2007

Bacterial luciferase is a heterodimeric enzyme, which catalyzes the light emission reaction, utilizing reduced FMN (FMNH2), a long chain aliphatic aldehyde and $O_2$, to produce green-blue light. This enzyme can be readily classed as slow or fast decay based on their rate of luminescence decay in a single turnover. Mutation of Glu175 in $\alpha$ subunit to Gly converted slow decay Xenorhabdus Luminescence luciferase to fast decay one. The following studies revealed that changing the luciferase flexibility and lake of Glu-flavin interactions are responsible for the unusual kinetic properties of mutant enzyme. Optical and thermodynamics studies have caused a decrease in free energy and anisotropy of mutant enzyme. Moreover, the role of Glu175 in transition state of folding pathway by use of stopped-flow fluorescence technique has been studied which suggesting that Glu175 is not involved in transition state of folding and appears as surface residue of the nucleus or as a member of one of a few alternative folding nuclei. These results suggest that mutation of Glu175 to Gly extended the structure of Xenorhabdus Luminescence luciferase, locally.

• BMB Reports
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• v.42 no.3
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• pp.166-171
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• 2009

Hsp70s assist in the process of protein folding through nucleotide-controlled cycles of substrate binding and release by alternating from an ATP-bound state in which the affinity for substrate is low to an ADP-bound state in which the affinity for substrate is high. It has been long recognized that the two-domain structure of Hsp70 is critical for these regulated interactions. Therefore, it is important to obtain information about conformational changes in the relative positions of Hsp70 domains caused by nucleotide binding. In this study, analytical ultracentrifugation and dynamic light scattering were used to evaluate the effect of ADP and ATP binding on the conformation of the human stress-induced Hsp70.1 protein. The results of these experiments showed that ATP had a larger effect on the conformation of Hsp70 than ADP. In agreement with previous biochemical experiments, our results suggest that conformational changes caused by nucleotide binding are a consequence of the movement in position of both nucleotide- and substrate-binding domains.

• Steel and Composite Structures
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• v.28 no.5
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• pp.607-615
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• 2018

The dynamic behavior of the deployment and folding process of a foldable boom based on the Miura origami pattern is investigated in this paper. Firstly, mechanical behavior of a single storey during the motion is studied numerically. Then the deployment and folding of a multi-storey boom is discussed. Moreover, the influence of the geometry parameters and the number of Miura-ori elements n on the dynamic behavior of the boom is also studied. Finally, the influence of the imperfection on the dynamic behavior is investigated. The results show that the angles between the diagonal folds and horizontal folds will have great effect on the strains during the motion. A bistable configuration can be obtained by choosing proper fold angles for a given multi-storey boom. The influence of the imperfection on the folding behavior of the foldable mast is significant.

• Animal cells and systems
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• v.7 no.3
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• pp.207-211
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• 2003

Caveolin-1 is a principal protein in the plasma membrane microdomains called caveolae. Caveolae play an important role in the transcytosis and pinocytosis. Therefore, caveolin-1 is most likely to work for the membrane dynamic events. In addition, caveolin-1 interacts with various signaling molecules. Although caveolin-1 possesses a variety of physiological functions, its structural properties were little construed. Here we analyzed the structural dynamics of the N-terminal caveolin-1 (residues 1-101), in order to better understand the structural properties in terms of its versatile functionality. We first analyzed its oligomeric form using GST-fused N-terminal domain, revealing that it equilibrates between a dimer and monomers in av concentration-dependent manner. The N-terminal domain of caveolin-1 was previously found to form a heptamer, so that our data suggest the dimeric form as an intermediate structure for the heptamer formation. Then, we obtained the folding profile, which indicated that $\DeltaG_{H2O}\;is\;about\;0.5\;\pm0.03$ kcal/mol. The stability of N-terminal domain is relatively low, indicating that N-terminal domain may not be crystalline. Conclusively, the dynamic and flexible structure of N-terminal domain appears more favorable to maintain the versatile functions of caveolin-1.

• BMB Reports
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• v.41 no.1
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• pp.35-40
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• 2008

The molten globular conformation of V26A ubiquitin (valine to alanine mutation at residue 26) was studied by nuclear magnetic resonance spectroscopy in conjunction with amide hydrogen/deuterium exchange. Most of the amide protons that are involved in the native secondary structures were observed to be protected in the molten globule state with the protection factors from 1.2 to 6.7. These protection factors are about 2 to 6 orders of magnitude smaller than those of the native state. These observations indicate that V26A molten globule has native-like backbone structure with marginal stability. The comparison of amide protection factors of V26A ubiquitin molten globule state with those of initial collapsed state of the wild type ubiquitin suggests that V26A ubiquitin molten globule state is located close to unfolded state in the folding reaction coordinate. It is considered that V26A ubiquitin molten globule is useful model to study early events in protein folding reaction.

• International journal of advanced smart convergence
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• v.8 no.1
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• pp.58-64
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• 2019

In recent years, small mobile devices called personal mobility or smart mobility have attracted attention. Personal mobility refers to electric-driven personal transportation that can travel at close range and medium distance, including small electric vehicles, electric bicycles, electric motorcycles and electric scooters. Most of the electric scooters used in Korea are mainly imported from China. This is due to the fact that the price competitiveness of major components of electric scooters is owned in China. At this point, the domestic research direction is preferable for the composition and design of the electric scooter body rather than cost reduction for the components. In this study, we propose a new model of portable folding structure that is easy to use for electric scooters, which are personal vehicles using electric energy. We also made a prototype for practical use.

• 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.