• Genomics & Informatics
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• v.2 no.4
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• pp.167-173
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• 2004

The main mechanism of evolution is that biological entities change, are selected, and reproduce. We propose a different concept in terms of the main agent or atom of evolution: in the biological world, not an individual object, but its interactive network is the fundamental unit of evolution. The interaction network is composed of interaction pairs of information objects that have order information. This indicates a paradigm shift from 3D biological objects to an abstract network of information entities as the primary agent of evolution. It forces us to change our views about how organisms evolve and therefore the methods we use to analyze evolution.

• Proceedings of the Korean Biophysical Society Conference
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• 1999.06a
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• pp.46-46
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• 1999

Positively charged cytochrome c interacts with the negatively charged mitochondrial inner membrane. This interaction induces conformational changes in bound cytochrome c. In order to estimate the effect of cytochrome c-membrane interaction on the mitochondrial electron transfer, we have investigated oxidation of ferrocytochrom c in the presence of anionic phospholipids.(omitted)

• Proceedings of the Zoological Society Korea Conference
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• 2000.04a
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• pp.75.2-75
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• 2000

No Abstract, See Full Text

• 한국전산유체공학회:학술대회논문집
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• 2006.05a
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• pp.149-149
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• 2006

• Proceedings of the Botanical Society of Korea Conference
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• 2002.04a
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• pp.91-91
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• 2002

• Proceedings of the Zoological Society Korea Conference
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• 2001.04a
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• pp.86.1-86
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• 2001

No Abstract, See Full Text

• Proceedings of the Zoological Society Korea Conference
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• 1997.10b
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• pp.227.1-227
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• 1997

No Abstract, See Full Text

• BMB Reports
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• v.50 no.5
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• pp.275-280
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• 2017

Herpes simplex virus type 1 ICP27 is a multifunctional protein responsible for viral replication, late gene expression, and reactivation from latency. ICP27 interacts with various cellular proteins, including Daxx. However, the role of interaction between ICP27 and Daxx is largely unknown. Since Daxx is known to repress $NF-{\kappa}B$ activity, there is a possibility that ICP27 may influence the inhibitory effect of Daxx on $NF-{\kappa}B$ activity. In this study, we tested whether ICP27 affects the $NF-{\kappa}B$ activity through its interaction with Daxx. Interestingly, ICP27 enhanced the Daxx-mediated repression of $NF-{\kappa}B$ activity. In addition, we found that sumoylation of Daxx regulates its interaction with p65. ICP27 binds to Daxx, inhibits Daxx sumoylation, and enhances p65 deacetylation induced by Daxx. Consequently, ICP27 represses the $NF-{\kappa}B$ activity, by elevating the inhibitory effect of Daxx on $NF-{\kappa}B$ activity through desumoylation of Daxx.

• Proceedings of the Microbiological Society of Korea Conference
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• 2000.10a
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• pp.39-45
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• 2000

It hab been proposed that CHS3-mediated chitin synthesis during the vegitative cell cycle is regulated by CHS4. To investigate direct protein-protein interaction between their coding products, we used yeast two hybrid system and found that a domain of Chs3p was responsible for interaction with Chs4p. This domain, termed MIRC3-4 (maximum interacting region of chs3p with chs4p), spans from 647 to 700 residues. It is well conserved among CHS3 homologs of various fungi such as Candida albicans, Emericella nidulans, Neurospora crassa, Magnaporthe grisea, Ustilago maydis, Glomus versiforme, Exophiala dermatitidis, Rhizopus microsporus. A series of mutaion in the MIRC3-4 resulted in no appearance of chitin ring at the early G 1 phase but did not affect chitin synthesis in the cell wall after cytokinesis. Absence of chitin ring could be caused either by delocalization of Chs3p to the septum or by improper interaction with Chs4p. To discriminate those two, not mutually exclusive, alternatives, mutants cells were immunostained with Chs3p-specific antibody. Some exhibited localization of chs3p to the septum, while others failed. These results indicate that simultaneous localization and activation Chs3p by Chs4p is required for chitin ring synthesis.

• Proceedings of the Korean Society of Precision Engineering Conference
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• 2005.06a
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• pp.641-644
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• 2005

The study on the interaction forces of some biological materials is important to understanding biological phenomena and their application to practical purpose. This paper introduces a measuring technique for biological adhesive forces using the AFM(Atomic Force Microscope). Since no standardized thesis on adhesive forces exist, the adhesive forces is defined as adhesive forces against a hardened surface of biological materials. To grant the results are meaningful, which is based on the understanding the surface characteristics of biological materials using the AFM, a nominal value of average adhesive force per unit area should be measured. Therefore the modified AFM probe with small micro glass bead was proposed so that it can guarantee the required contact area for measuring the average adhesive forces. A pyrex glass substrate with circular patterns, which was fabricated by micromachining technique, is introduced in order to controll the contact area. The two types of mussel adhesive proteins, Celltak and recombinant-MGFP5, were tested by the proposed measuring method. The test results show that the adhesive force of the mussel adhesive proteins can be reliably measured by use of this method.