• Preventive Nutrition and Food Science
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• v.21 no.1
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• pp.1-8
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• 2016

Increasing knowledge on the link between diet and human health has generated a lot of interest in the development of functional foods. However, several challenges, including discovering of beneficial compounds, establishing optimal intake levels, and developing adequate food delivering matrix and product formulations, need to be addressed. A number of new processes and materials derived from nanotechnology have the potential to provide new solutions in many of these fronts. Nanotechnology is concerned with the manipulation of materials at the atomic and molecular scales to create structures that are less than 100 nm in size in one dimension. By carefully choosing the molecular components, it seems possible to design particles with different surface properties. Several food-based nanodelivery vehicles, such as protein-polysaccharide coacervates, multiple emulsions, liposomes and cochleates have been developed on a laboratory scale, but there have been very limited applications in real food systems. There are also public concerns about potential negative effects of nanotechnology-based delivery systems on human health. This paper provides an overview of the new opportunities and challenges for nanotechnology-based systems in future functional food development.

• Bulletin of the Korean Chemical Society
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• v.33 no.10
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• pp.3378-3382
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• 2012

A superhydrophobic surface with a water contact angle > $150^{\circ}$ has attracted great interest from both fundamental and practical aspects. In this study, we demonstrated that hydrophobicity of a silica nanotube (SNT) array can be easily controlled by the SNT aspect ratio. In addition, the adhesive and anti-adhesive properties were controlled without modifying the hydrophobic surface. Various silica structures on a polydimethylsiloxane substrate were prepared using the desired alumina template. Bundle-arrayed and bowl-arrayed silica surfaces exhibited extraordinary superhydrophobicity due to the large frontal surface area and hierarchical micro/nanostructure. As the strategy used in this study is biocompatible and a wide range of hydrophobicities are capable of being controlled by the SNT aspect ratio, a hydrophobic surface composed of an SNT array could be an attractive candidate for bioapplications, such as cell and protein chips.

• Bulletin of the Korean Chemical Society
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• v.24 no.6
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• pp.785-791
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• 2003

We have studied the folding mechanism of β-hairpins from proteins of 1GB1, 3AIT and 1A2P by unfolding simulations at high temperatures. The analysis of trajectories obtained from molecular dynamics simulations in explicit aqueous solution suggests that the three β-hairpin structures follow different mechanism of folding. The results of unfolding simulations showed that the positions of the hydrophobic core residues influence the folding dynamics. We discussed the characteristics of different mechanisms of β-hairpin folding based on the hydrogen-bond-centric and the hydrophobic-centric models.

• Korean Journal of Veterinary Service
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• v.30 no.4
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• pp.539-544
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• 2007

A 7-year-old intact female Golden Retriever was presented for examination. The dog had large irregular subcutaneous masses in the abdomen which were ruptured or encapsulated. Those were removed surgically. Histopathologically, the masses consisted of spindle cells that often formed distinct whorls around a central capillary. Immuno-histochemical analysis revealed that the neoplastic cells were strong diffuse cyto-plasmic immunolabelling for vimentin and focal immunoreactivity for smooth muscle actin, whereas not immunoreactive for cytokeratin, desmin, von Willebrand factor, glial fibrillary acidic protein, or S-100. The neoplastic cells ultrastructurally had processes attached by desmosome-like structures, swollen mitochondria and dilated rough endoplasmic reticulum. Based on the above results, this case was diagnosed as a canine hemangiopericytoma in the abdominal subcutis of a Golden Retriever.

• Applied Biological Chemistry
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• v.41 no.8
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• pp.568-571
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• 1998

The conformations of human insulin precursors, proinsulin and preproinsulin, are described in terms of molecular dynamics simulations. Despite the presence of the C-peptide and/or the signal peptide, molecular dynamics calculations utilizing the hydration shell model over a period of 500 ps indicate that the native conformations of the A and B chains are well conserved in both cases. These results further support the NMR spectroscopy results that the C-peptide is relatively disordered and does not influence the overall conformation of the native structure. The robustness of the native structure as demonstrated by experiment and simulation will permit future protein engineering applications, whereby the expression or purification yields can be improved upon sequence modification of the C-peptide and/or the signal peptide.

• Journal of the Korean Magnetic Resonance Society
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• v.18 no.1
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• pp.5-9
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• 2014

In last three decades, RNA molecules have been revealed to play the central roles in many cellular processes. Structural understanding of RNA molecules is essential to interpret their functions, and many biophysical techniques have been adopted for this purpose. NMR spectroscopy is a powerful tool to study structures and dynamics of RNA molecules, and it has been further applied to study tertiary interactions between RNA molecules, RNA-protein, and RNA-small molecules. This short article accounts for the general methods for NMR sample preparations, and also partially covers the resonance assignments of structured RNA molecules.

• Journal of the Korean Society of Clothing and Textiles
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• v.35 no.6
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• pp.670-677
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• 2011

This study is to optimize the enzymatic processing conditions of Polylactic Acid (PLA) fiber using lipase from Porcine pancreas as an environmental technology. Hydrolytic activity dependent on pH, temperature, enzyme concentration, and treatment time, and structural change of PLA fiber were evaluated. The PLA fiber hydrolysis by lipase was maximized at 50% (o.w.f) lipase concentration $50^{\circ}C$ for 120 minutes under pH 8.5. There was a change of the protein absorbance in the treatment solution before and after the lipase treatment. In addition, there was no substantial change in the molecular and crystalline structures of PLA by lipase treatment as confirmed by DSC, XRD, and FT-IR.

• Journal of Microbiology and Biotechnology
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• v.9 no.2
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• pp.219-222
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• 1999

A simple sequence of membrane concentration and DEAE-Cellulose chromatography has been optimized to give a purified dextransucrase from Leuconostoc mesenteroides B-512FMCM with the highest specific activity (248.8 IU/mg protein) ever reported in high yield (overall 88.7%) for dextransucrase. When there was no sucrose in the dextransucrase and the dextran reaction digest, the dextransucrase hydrolyzed glucose from dextran. The glucose was transferred to the other glucoses from dextran and formed isomaltose and isomaltodextrin. The transglycosylation efficiency of glucose from dextran was much higher with acceptors. The dextransucrase can be used for the production of various kinds (or structures) of oligosaccharides using dextran and various acceptors with almost 100% theoretical yield.

• Journal of the Korean Magnetic Resonance Society
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• v.13 no.1
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• pp.56-63
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• 2009

SWIRM domain, a core domain of SRG3 is well conserved in SW13, RSC8, and MOIRA family proteins. To understand structural basis for cellular functions of the SWIRM domain, we have initiated biochemical and structural studies on SWIRM domain and mutants using gelfiltration chromatography, circular dichroism and NMR spectroscopy. The structural properties of the mutant SWIRM domains (K34A and M75A) have been characterized, showing that the structures of both wild-type and mutant proteins are a-helical conformation. The data conclude that mutations at interaction sites of its binding partner protein do not affect its secondary and tertiary structure.

• Journal of the Korean Magnetic Resonance Society
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• v.24 no.2
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• pp.47-52
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• 2020

Liquid-liquid phase separation (LLPS) of biomolecules, a newly-found phase behavior of molecules in the liquid phase, has shown to its relationship to various biological function and misfolding diseases. Extensive studies have increasingly revealed a general mechanism of LLPS and characterized the liquid droplet; ho wever, intermolecular interactions of proteins and structural states of LLPS-inducing proteins inside of the droplet remain largely unknown. Solution NMR spectroscopy has emerged as a powerful approach as it provides invaluable information on protein intermolecular interactions and structures at the atomic and residue level. We herein comprehensively address useful techniques of solution NMR including the effect of paramagnetic relaxation enhancement for the study on the LLPS and droplet based on recent studies.