• 한국HCI학회:학술대회논문집
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• 2007.02a
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• pp.32-37
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• 2007

기존의 CAVE 를 이용한 분자구조 visualization 혹은 교육 시스템에서는 CAVE 시스템의 특징을 반영하지 않은 desktop 방식의 상호작용(interaction) 방법과 조망(viewing) 방법을 제공했다. 이러한 기존의 방법들은 CAVE 시스템의 장점을 충분히 이용하지 못한 것이다. 우리는 사용자에게 CAVE 시스템의 장점을 잘 살릴 수 있는 일인칭 시점의 조망을 제공하는 분자구조 교육 시스템을 개발함으로써 사용자에게 좀더 교육적으로나 경험적으로 효과가 큰 분자구조 교육 시스템을 제안한다. 또한 간단한 실험을 통해서 우리가 제안한 시스템의 효과를 알아보았다.

• Applied Microscopy
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• v.20 no.2
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• pp.57-70
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• 1990

Characterization and electron microscopic visualization of the plasmid and the gene expression of Escherichia coli were carried out. Transcriptional units of active structural genes were observed after lysis of Escherichia coli cells. The ribosomes attached to the E. coli genome on mRNA molecule as polyribosomes. From this gradient of polyribosome length, we estimated location of mRNA synthesis initiation site. In this experiment, a granule is ofen present which may correspond to a RNA polymerase at the promoter site. pOX1, pOX7, pOX7A, $pOX7{\Delta}1$, pSTP36, pSTP21, pBR322, and pJH12 were visualized by way of electron microscope, and their estimated sizes were determined to be $5.70{\pm}0.08{\mu}m,\;2.15{\pm}0.10{\mu}m,\;2.14{\pm}0.12{\mu}m,\;7.39{\pm}0.08{\mu}m,\;4.03{\pm}0.04{\mu}m,\;1.50{\pm}0.03{\mu}m\;and\;1.25{\pm}0.09{\mu}m$ respectively. One micrometer of measured length corresponded to about 3.0 Kb. Mica-press adsorption method that allows selectivs visualization of the plasmid DNA released in situ from the bacterial cell is rapid and useful for visualization of plasmids. The released plasmid DNA was adsorbed preferently on mica in a divalent cation-free solution. Miller chromatin-spreading method was useful to observe the plasmid and transcripts. BAC method and cytochrome C monolayer were useful to observe the plasmid DNA. Our ability to visualize ultrastructural aspects of the expression of E. coli has given us a unique tool with which to study the regulation the level of an individual gene.

• Biomolecules & Therapeutics
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• v.26 no.2
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• pp.182-190
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• 2018

The objective of this work is to evaluate the effect of polyamidoamine (PAMAM) dendrimers on electroosmotic flow (EOF) through skin. The effect of size and concentration of dendrimer was studied, using generation 1, 4 and 7 dendrimer (G1, G4 and G7, respectively). As a marker molecule for the direction and magnitude of EOF, a neutral molecule, acetoaminophen (AAP) was used. The visualization of dendrimer permeation into the current conducting pore (CCP) of skin was made using G4-fluorescein isothiocyanate (FITC) conjugate and confocal microscopy. Without dendrimer, anodal flux of AAP was much higher than cathodal or passive flux. When G1 dendrimer was added, anodal flux decreased, presumably due to the decrease in EOF by the association of G1 dendrimer with net negative charge in CCP. As the generation increased, larger decrease in anodal flux was observed, and the direction of EOF was reversed. Small amount of methanol used for the preparation of dendrimer solution also contributed to the decrease in anodal flux of AAP. Cross-sectional view perpendicular to the skin surface by confocal laser scanning microscope (CLSM) study showed that G4 dendrimer-FITC conjugate (G4-FITC) can penetrate into the viable epidermis and dermis under anodal current. The permeation route seemed to be localized on hair follicle region. These results suggest that PAMAM dendrimers can permeate into CCP and change the magnitude and direction of EOF. Overall, we obtained a better understanding on the mechanistic insights into the electroosmosis phenomena and its role on flux during iontophoresis.

• KIPS Transactions on Software and Data Engineering
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• v.2 no.12
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• pp.899-902
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• 2013

In this paper, we present a method to visualize the contact region between two molecules in a protein complex in a threedimensional space. The contact region of two molecules shows compatibility in geometric aspects. Usually, the computation of the area of contact region has been used to show the strength of compatibility. The numerical value and simple drawing of contact region would be useful for comparing the relative strength of different contacts, but it is not appropriate for analysing the geometric characteristics of the contact region. In this paper, we present a method to show the compatibility between two molecules by visualizing the distance information between them.

• The KIPS Transactions:PartD
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• v.11D no.7 s.96
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• pp.1517-1526
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• 2004

Entering the post genome era with an increasing amount of protein data available in public databases, the study of tertiary structure of pro-teins has been artively in progress. To analyze the structure of a protein effectively, it is necessary to visualize the tertiary structure of a protein. Rececntly, many visualization tools based on Java technology have been developed to visualize a protein whose structure has been known. In this paper, we describe a new protein visualization system, named JProtein. It is designed to be an easy-to-use, platform neutral melocular visualization tool. The JProtein system is developed using Java3D technology. Java3D is an API providing a programming interface for 3D representations. The system informs us the angle and the distance of the interacting atoms in amino acids which are visualized, providing several 3D representation models of a protein molecule. In particular, the JProtein system presents synchronous stereo view as well as asynchronous one.

• Vacuum Magazine
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• v.4 no.4
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• pp.18-22
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• 2017

Transmission electron microscopy (TEM) is a versatile and powerful technique that enables direct visualization of biological samples of sizes ranging from whole cell to near-atomic resolution details of a protein molecule. Thanks to numerous technical breakthroughs and monumental discoveries, 3D electron microscopy (3DEM) has become an indispensable tool in the field of structural biology. In particular, development of cryo-electron microscopy(cryo-EM) and computational image processing played pivotal role for the determination of 3D structures of complex biological systems at sub-molecular resolution. Here, basis of TEM and 3DEM will be introduced, especially focusing on technical advancements and practical applications. Also, future prospective of constantly evolving 3DEM field will be discussed, with an anticipation of great biological discoveries that were once considered impossible.

• Journal of the Korean Society of Visualization
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• v.20 no.3
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• pp.136-145
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• 2022

Later flow immunoassay (LFIA) is a protein analytical method based on immunoreaction. On the LFIA based protein analytical method, bioreceptor molecule plays a key role, and so a system that evaluates and manages the binding affinity of bioreceptor is needed to secure detection reliability. In this study, Lateral Flow Immunoassay based rapid Bioreceptor Screening Method (rBSM) is presented that provide a simple and quick evaluating method for the binding affinity to the target protein of the antibody as model bioreceptor. To verify this evaluation method, Virus-like particles (VLP) and anti-VLP antibodies are selected as a model norovirus, which is target protein, and the candidate bioreceptors respectively. Among the 5 different candidate antibodies, appropriate antibody could be sorted out within 30 minutes through rBSM. In addition, selected antibodies were applied to two representative LFIA based techniques, sandwich assay and competitive assay. Among these methods, sandwich assay showed more effective VLP detection method. Through applying selected antibodies and techniques to the commercialized mass production lines, an VLP detecting LFIA kit was developed with a detection limit of 10¹² copies/g of VLPs in real samples. Since this proposed method in this study could be easily transformable into other combinations with bioreceptors, it is expected that this technique would be applied to LFIA kit development system and bioreceptor quality management.