• Biotechnology and Bioprocess Engineering:BBE
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• v.8 no.1
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• pp.9-18
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• 2003

The most challenging and emerging field of biotechnology is the tailoring of proteins to attain the desired characteristic properties. In order to increase the stability of proteins and to study the function of proteins, the mechanism by which proteins fold and unfold should be known. It has been debated for a long time how exactly the linear form of a protein is converted into a stable 3-dimensional structure. The literature showed that many theories support the fact that protein folding E5 a Thermodynamically controlled process. It is also possible to predict the mechanism of protein deactivation and Stability to an extent from thermodynamic studies. This article reviewed various theories that have been proposed to explain the process of protein folding after its biosynthesis in ribosomes. The theories of the determination of the thermodynamic properties and the interpretation of thermodynamic data of protein stability are 3150 discussed in this article.

• BMB Reports
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• v.54 no.5
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• pp.233-245
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• 2021

In eukaryotes, the genome is hierarchically packed inside the nucleus, which facilitates physical contact between cis-regulatory elements (CREs), such as enhancers and promoters. Accumulating evidence highlights the critical role of higher-order chromatin structure in precise regulation of spatiotemporal gene expression under diverse biological contexts including lineage commitment and cell activation by external stimulus. Genomics and imaging-based technologies, such as Hi-C and DNA fluorescence in situ hybridization (FISH), have revealed the key principles of genome folding, while newly developed tools focus on improvement in resolution, throughput and modality at single-cell and population levels, and challenge the knowledge obtained through conventional approaches. In this review, we discuss recent advances in our understanding of principles of higher-order chromosome conformation and technologies to investigate 4D chromatin interactions.

• Biomedical Science Letters
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• v.11 no.1
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• pp.85-88
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• 2005

Hemoglobin is oxygen carrier protein within erythrocyte in blood. Apoprotein of this, globin, is synthesized in the cytosol but it's cofactor, heme, is synthesized in the mitochondria. It has not been known very well how globin receives the heme from mitochondria and folds to hemoglobin. In this folding process, the initial structure of globin seems to be very important. A small volume of globin at acid pH was added rapidly into the bulk of an egg phosphatidylcholine $60\%$ liposome, containing hemins, at neutral pH according to the Rapid Dilution method. It was observed that an acid-induced unfolding structure of globin is initially needed to receive hemins from the lipid bilayer of liposomes. Also, this conclusion was confirmed with the absorption spectrum of the refolded globin separated by centrifugation.

• Proceedings of the Korean Geotechical Society Conference
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• 2002.10a
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• pp.507-512
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• 2002

Generally gneiss regions catagolized as metamorphic ground are very complicated and difficult for geotenical engineer to establish stability, this slopes include falt zone and many folding structures. therefore the slope in this study is very complicated and highly wheathered and framentation conditions are irregular by this study, we hope that geotechical engineers who are confronted with the same complicated slope as this slope are doing his job easily and they know which system are adequate to establish the slope stability in large-scale slope with complicated geological structure, and besides through our work flow and modeling process, we hope that our study can be useful for geotenical engineer who may work slope design and construct in complicated ground.

• The Research Journal of the Costume Culture
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• v.20 no.2
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• pp.222-237
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• 2012

Air-containing fashion, which can offer diverse functions through the inflow and outflow of air, is highly relevant in today's mobile society, where people are experiencing a wider range of environments. This study attempts to suggest the possibility of air-containing multi-functional fashion that could continuously be utilized by developing a design for an air-containing jacket using modular systems. In this research, the modular systems in architecture and furniture design were referenced through a review of the literature for the purpose of establishing modular systems in fashion. Functions relevant to the mobility of today's society are derived from the results of advanced research and applied to the design of modules of the jacket. The modules are integrated through the modular systems. The folding and unfolding structure in architecture and furniture is applied as a folding system in fashion, the vertical accumulation structure as a layering system, and the horizontal integration structure as a combining system, and in addition, the containing system has emerged in fashion. Each module is designed to fulfill certain functions, such as cushioning, heat insulation, and portability. The folding system is utilized in designing the cushion module to support the neck and back of a wearer by making its hood and hem fold in the back. The application of a layering system was suggested by making the vest, combined with the neck cushion and back cushion via the combining system, layered with its insulation module. By applying the combining system, the hood that includes the neck cushion, the skirt that includes the back cushion, the body that includes the insulation module, and the sleeves can be connected and separated by a zipper. The applicability of this concept was proven by applying a developed design to an actual item.

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2003.04a
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• pp.44-44
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• 2003

Protein disulfide isomerase (PDI) is not only an isomerase catalyzing the formation of native disulfide bond(s) of nascent peptide, but also a molecular chaperone assisting chain folding. We have already reported the structure of a cDNA (bPDl) encoding PDI from Bombyx mori and the function of PDI as foldase in assisting protein folding. (omitted)

• Korean Journal of Microbiology
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• v.25 no.2
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• pp.94-102
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• 1987

Rat liver LDH A-cDNA has been isolated from a .lambda.gt11-rat lover cDNA library and partially characterized. The size of the isolated rat liver LDH A-cDNA if shown to be 1.6Kb and restriction enzyme sites for the rat liver LDH A-cDNA are also mapped. 682-nucleotide sequence coding for 3'-end of rat liver LDH A-cDNA has been analyzed and compared to the nucleotide sequence of the same region of rat $C_6$-glioma cell LDH A-cDNA which has been cloned from the hormonally stimulated cell cultures. The result shows that 177 nucleotide sequences coding for the C-terminal 59-amino acids are identical but 505 nucleotide sequences of 3'-nontranslated region of the two LSH A-cDNA exhibit characteristic differences in thier nucleotide sequences. Computer analysis for the folding structures for 3'-end 400 nucleotide sequences of the two LDH A-cDNA shows a possibility implying that the two LDH A-mRNAs isolated from different tissues of rats may have different half life and therefore their translational efficiency may be different. It has been previously demonstrated that isoproterenol stimulated rat $C_6$ -glioma cell cultures produce LDH A-mRNA showing 2 to 3-fold longer half life in comparison to that of noninduced LHD A-mRNA. The result therefore support for the idea that hormonally stimulated rat $C_6$-glioma cells may produce LDH A-mRNA containing different nucleotide sequences at the 3'-end nontranslated region by which the hormonally induced LDH A-mRNA could have more stable secondary mRAN structure in comparison to that of noninduced LDH A-mRNA.

• BMB Reports
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• v.32 no.6
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• pp.521-528
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• 1999

The folding of recombinant hepatitis B virus X-protein (rHBx) solubilized from Escherichia coli inclusion bodies was investigated. By sequential dialysis of urea, rHBx was folded into its native structure, which was demonstrated by the efficacy of its transcriptional activation of the adenovirus major late promoter (MLP), fluorescence spectroscopy, and circular dichroism (CD) analysis. The decrease in CD values at 220 nm and a corresponding blue shift of the intrinsic fluorescence emission confirmed the ability of rHBx to refold in lower concentrations of urea, yielding the active protein. Equilibrium and kinetic studies of the refolding of rHBx were carried out by tryptophan fluorescence measurements. From the biphasic nature of the fluorescence curves, the existence of stable intermediate states in the renaturation process was inferred. Reverse phase-high performance liquid chromatography (RP-HPLC) analysis further demonstrated the existence of these intermediates and their apparent compactness.

• Journal of Engineering Education Research
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• v.22 no.5
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• pp.49-55
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• 2019

Folded structure is widely applied in various engineering fields. Many of the Japanese folding fans in the Edo era (1603-1868) have been successfully blended with the processing technology of "natural materials" that is the origin of Japan's "Monodzukuri" (craftsmanship) and its application "artistic originality". The charm of a fan lies in the diversity of stereoscopic expression not born in plane representation. For example, the effects of folds, the expression of the front and back sides flowing from the front to the back by double-sided description, and the two-layer effect of raising the backside from the surface using the permeability of Japanese paper, the calculated depiction are also seen. Moreover, by handling the fan, it also produced an illusion effect which skillfully calculated the change due to movement of the viewpoint. Students experience the natural materials such as Japanese paper, bamboo and starch paste, which are the materials of paint and fan at the time, and processing method, and know the difference with the current one. This study is to verify the effectiveness of engineering education which gains experience by making concrete fans and to understand deeply this traditional technology with the artistry of a Japanese fan at the same time. And we can learn from the characteristics of the fan to Japan's history and culture.

• Bulletin of the Korean Chemical Society
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• v.35 no.6
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• pp.1713-1719
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• 2014

1FSD is a 28-residue designed protein with a ${\beta}{\beta}{\alpha}$ motif. Since this protein displays most essential features of protein structures in such a small size, this model protein can be an outstanding system for evaluating the balance in the propensity of the secondary structures and the quality of all-atom protein force fields. Particularly, this protein would be difficult to fold to its correct native structure without establishing proper balances between the secondary structure elements in all-atom energy functions. In this work, a series of the recently optimized five amber protein force fields [$ff03^*$, $f99sb^*$-ildn, ff99sb-${\phi}^{\prime}$-ildn, ff99sb-nmr1-ildn, ff99sb-${\Phi}{\Psi}$(G24, CS)-ildn] were investigated for the simulations of 1FSD using a conventional molecular dynamics (MD) and a biased-exchange meta-dynamics (BEMD) methods. Among those tested force fields, we found that ff99sb-nmr1-ildn and ff99sb-${\Phi}{\Psi}$(G24, CS)-ildn are promising in that both force fields can locate the native state of 1FSD with a high accuracy (backbone rmsd ${\leq}1.7{\AA}$) in the global free energy minimum basin with a reasonable energetics conforming to a previous circular dichroism (CD) experiment. Furthermore, both force fields led to a common set of two distinct folding pathways with a heterogeneous nature of the transition state to the folding. We anticipate that these force fields are reasonably well balanced, thereby transferable to many other protein folds.