• Applied Microscopy
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• v.47 no.3
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• pp.165-170
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• 2017

Gas vesicles are intracellular gas-filled protein-shelled nanocompartments. The structures are spindle or cylinder-shaped, and typically $0.1{\sim}2{\mu}m$ in length and 45~250 nm in width. A variety of prokaryotes including photosynthetic bacteria and halophilic archaea form gas vesicles in their cytoplasm. Gas vesicles provide cell buoyancy as flotation devices in aqueous habitats. They are used as nanoscale molecular reporters for ultrasound imaging for biomedical purposes. The structures in halophilic archaea are poorly resolved due to the low signal-to-noise ratio from the high salt concentration in the medium. Such a limitation can be overcome using focused ion beam-thinning or inelastically scattered electrons. As the concentric bodies (~200 nm in diameter) in fungi possess gas-filled cores, it is possible that the concept of gas vesicles could be applied to eukaryotic microbes beyond prokaryotes.

• BMB Reports
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• v.41 no.5
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• pp.353-357
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• 2008

LRR family proteins play important roles in a variety of physiological processes. To facilitate their production and crystallization, we have invented a novel method termed "Hybrid LRR Technique". Using this technique, the first crystal structures of three TLR family proteins could be determined. In this review, design principles and application of the technique to protein crystallization will be summarized. For crystallization of TLRs, hagfish VLR receptors were chosen as the fusion partners and the TLR and the VLR fragments were fused at the conserved LxxLxLxxN motif to minimize local structural incompatibility. TLR-VLR hybridization did not disturb structures and functions of the target TLR proteins. The Hybrid LRR Technique is a general technique that can be applied to structural studies of other LRR proteins. It may also have broader application in biochemical and medical application of LRR proteins by modifying them without compromising their structural integrity.

• Biomolecules & Therapeutics
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• v.29 no.6
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• pp.605-614
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• 2021

Autophagy is an important degradative pathway that eliminates misfolded proteins and damaged organelles from cells. Autophagy is crucial for neuronal homeostasis and function. A lack of or deficiency in autophagy leads to the accumulation of protein aggregates, which are associated with several neurodegenerative diseases. Compared with non-neuronal cells, neurons exhibit rapid autophagic flux because damaged organelles or protein aggregates cannot be diluted in post-mitotic cells; because of this, these cells exhibit characteristic features of autophagy, such as compartment-specific autophagy, which depends on polarized structures and rapid autophagy flux. In addition, neurons exhibit compartment-specific autophagy, which depends on polarized structures. Neuronal autophagy may have additional physiological roles other than amino acid recycling. In this review, we focus on the characteristics and regulatory factors of neuronal autophagy. We also describe intracellular selective autophagy in neurons and its association with neurodegenerative diseases.

• Journal of the Korean Society for Precision Engineering
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• v.29 no.11
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• pp.1245-1255
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• 2012

Effective elastic constants of biomimetic multilayer structures with hierarchical structures are evaluated based on the potential energy balance method. The effective anisotropic elastic constants are used in analyzing low-velocity impact of biomimetic multilayer structures consisting of mineral and protein. It is shown that displacements of biomimetic multilayer structures strongly depend on the volume fraction of mineral and hierarchical level. The effect of the volume fraction of mineral and hierarchical level on the contact force and stresses at the impact point are also discussed.

• Proceedings of the Korean Society for Bioinformatics Conference
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• 2003.10a
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• pp.268-274
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• 2003

Most currently known molecular structures were determined by X-ray crystallography or Nuclear Magnetic Resonance (NMR). These methods generate a large amount of structure data, even far small molecules, and consist mainly of three-dimensional atomic coordinates. These are useful for analyzing molecular structure, but structure elements at higher level are also needed for a complete understanding of structure, and especially for structure prediction. Computational approaches exist for identifying secondary structural elements in proteins from atomic coordinates. However, similar methods have not been developed for RNA due in part to the very small amount of structure data so far available, and extracting the structural elements of RNA requires substantial manual work. Since the number of three-dimensional RNA structures is increasing, a more systematic and automated method is needed. We have developed a set of algorithms for recognizing secondary and tertiary structural elements in RNA molecules and in the protein-RNA structures in protein data banks (PDB). The present work represents the first attempt at extracting RNA structure elements from atomic coordinates in structure databases. The regularities in the structure elements revealed by the algorithms should provide useful information for predicting the structure of RNA molecules bound to proteins.

• Journal of Plant Biotechnology
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• v.37 no.3
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• pp.292-304
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• 2010

High value-added therapeutic proteins have been leading the biologics industry and occupied major portion of the market. More than 60% of the currently available protein therapeutics are glycoproteins attached with glycans which play crucial roles for the protein folding, therapeutic efficacy, in vivo half-life and immunogenecity. This review introduces the process of glycosylation and the impacts of glycans in the aspects of therapeutics. The important glycan structures in therapeutic performances were also summarized focusing on three representative categories of glycoproteins, cytokines, therapeutic antibody and enzyme. Currently, mammalian expression systems such as Chinese hamster ovary cells are preferred for the production of therapeutic glycoproteins due to their ability to synthesize glycans having similar structures with human type glycans. However, recent advances of plant glycoengineering to overcome the limitation originating from different glycan structures will soon allow to develop more efficient and economic plant-based production systems for therapeutic glycoproteins.

• Bulletin of the Korean Chemical Society
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• v.33 no.8
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• pp.2508-2512
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• 2012

Cold shock proteins (CSPs) are a family of proteins induced at low temperatures. CSPs bind to single-stranded nucleic acids through the ribonucleoprotein 1 and 2 (RNP 1 and 2) binding motifs. CSPs play an essential role in cold adaptation by regulating transcription and translation via molecular chaperones. The solution nuclear magnetic resonance (NMR) or X-ray crystal structures of several CSPs from various microorganisms have been determined, but structural characteristics of psychrophilic CSPs have not been studied. Therefore, we optimized the purification process to obtain highly pure Lm-Csp and determined the three-dimensional structure model of Lm-Csp by comparative homology modeling using MODELLER on the basis of the solution NMR structure of Bs-CspB. Lm-Csp consists of a ${\beta}$-barrel structure, which includes antiparallel ${\beta}$ strands (G4-N10, F15-I18, V26-H29, A46-D50, and P58-Q64). The template protein, Bs-CspB, shares a similar ${\beta}$ sheet structure and an identical chain fold to Lm-Csp. However, the sheets in Lm-Csp were much shorter than those of Bs-CspB. The Lm-Csp side chains, E2 and R20 form a salt bridge, thus, stabilizing the Lm-Csp structure. To evaluate the contribution of this ionic interaction as well as that of the hydrophobic patch on protein stability, we investigated the secondary structures of wild type and mutant protein (W8, F15, and R20) of Lm-Csp using circular dichroism (CD) spectroscopy. The results showed that solvent-exposed aromatic side chains as well as residues participating in ionic interactions are very important for structural stability. Further studies on the three-dimensional structure and dynamics of Lm-Csp using NMR spectroscopy are required.

• The KIPS Transactions:PartD
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• v.8D no.5
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• pp.553-560
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• 2001

Bioinformatics is a discipline to support biological experiment projects by storing, managing data arising from genome research. In can also lead the experimental design for genome function prediction and regulation. Among various approaches of the genome research, the proteomics have been drawing increasing attention since it deals with the final product of genomes, i.e., proteins, directly. This paper proposes a data mining technique to predict the structural characteristics of a given protein group, one of dominant factors of the functions of them. After explains associations among amino acid subsequences in the primary structures of proteins, which can provide important clues for determining secondary or tertiary structures of them, it defines a sequence association rule to represent the inter-subsequences. It also provides support and confidence measures, newly designed to evaluate the usefulness of sequence association rules, After is proposes a method to discover useful sequence association rules from a given protein group, it evaluates the performance of the proposed method with protein sequence data from the SWISS-PROT protein database.

• Proceedings of the Korean Magnestics Society Conference
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• 2007.05a
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• pp.93.2-93.2
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• 2007

• Proceedings of the Korean Magnetic Resonance Society Conference
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• 2000.08a
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• pp.25-25
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• 2000