• Journal of Life Science
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• v.8 no.2
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• pp.223-233
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• 1998

Discovery of molecular chaperone has stimulate cell biologists and thus made it possible to re-examine the processes whereby proteins achieve and maintain their functional conformations within living cells. the term ‘Molecular chaperone’ was first coined to describe one particular protein involved in the assembly of nucleosomes, but the term has now been extended to describe the function of a wide variety of proteins that assist protein transport across membranes, folding of nascent polypeptide, the assembly and disassembly of oligomeric structures, and the recovery or removal of proteins damaged by various environmental stresses including heat shock. Progress of molecular chaperone research is still limited by the lack of 3-dimensional structural information and detailed interacts with taget proteins in the cell. However, several laboratories around the world are attempting to extend our knowledge on the functions of molecular chaperone, and such efforts seem justified to finally provide the answers to the most burning questions shortly.

• Journal of Life Science
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• v.8 no.2
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• pp.226-226
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• 1998

Discovery of molecular chaperone has stimulate cell biologists and thus made it possible to re-examine the processes whereby proteins achieve and maintain their functional conformations within living cells. the term ‘Molecular chaperone’ was first coined to describe one particular protein involved in the assembly of nucleosomes, but the term has now been extended to describe the function of a wide variety of proteins that assist protein transport across membranes, folding of nascent polypeptide, the assembly and disassembly of oligomeric structures, and the recovery or removal of proteins damaged by various environmental stresses including heat shock. Progress of molecular chaperone research is still limited by the lack of 3-dimensional structural information and detailed interacts with taget proteins in the cell. However, several laboratories around the world are attempting to extend our knowledge on the functions of molecular chaperone, and such efforts seem justified to finally provide the answers to the most burning questions shortly.

• Bulletin of the Korean Chemical Society
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• v.27 no.11
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• pp.1894-1896
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• 2006

• Proceedings of the Korean Vacuum Society Conference
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• 2011.02a
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• pp.24-25
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• 2011

Molecular self-assembly has several advantages over other nanofabrication methods. Molecular building blocks ensure ultrafine pattern precision, parallel structure formation allows for mass production and a variety of three-dimensional structures are available for fabricating complex structures. Nevertheless, the molecular interaction for self-assembly generally relies on weak forces such as van der Waals force, hydrogen bonding, or hydrophobic interaction. Due to the weak interaction, the structure formation is usually slow and the degree of ordering is low in a self-assembled structure. To promote self-assembly, directed assembly methods employing prepatterned substrates or external fields have been developed and gathered a great deal of technological attention as a next generation nanofabrication process. In this presentation a variety of directed assembly methods for soft nanomaterials including block copolymers, peptides and carbon nanomaterials will be introduced. Block copolymers are representative self-assembling materials extensively utilized in nanofabrication. In contrast to colloid assembly or anodized metal oxides, various shapes of nanostructures, including lines or interconnected networks, can be generated with a precise tunability over their shape and size. Applying prepatterned substrates$^{1,2}$ or introducing thickness modulation$^3$ to block copolymer thin films allowed for the control over the orientational and positional orderings of self-assembled structures. The nanofabrication processes for metals, semiconductors$^4$, carbon nanotubes$^{5,6}$, and graphene$^{6,7}$ templating block copolymer self-assembly will be presented.

• Bulletin of the Korean Chemical Society
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• v.24 no.7
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• pp.889-890
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• 2003

• Proceedings of the Korean Vacuum Society Conference
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• 2011.08a
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• pp.205-205
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• 2011

The self-assembly of ${\gamma}$-phenylalanine on Au(111) at 150 K was investigated using scanning tunneling microscopy (STM). Phenylalanine can potentially form two-dimensional (2D) molecular networks through hydrogen bonding (through the carboxyl and amino groups) and ${\pi}-{\pi}$ stacking interactions (via aromatic rings). We found that ${\gamma}$-phenylalanine molecules self-assembled on Au(111) surfaces into well-ordered structures such as ring-shaped clusters (at low and intermediate coverages) and 2D molecular domains (intermediate and monolayer coverages), whereas ${\alpha}$-phenylalanine molecules formed less-ordered structure on Au(111). The self-assembly of ${\gamma}$- but not ${\alpha}$-phenylalanine may be related to the flexibility of the carboxyl and amino groups in the molecule. Moreover, as expected, the 2D molecular network of ${\gamma}$-phenylalanine on Au(111) was mediated by a combination of hydrogen bonding and ${\pi}-{\pi}$ stacking interactions.

• BMB Reports
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• v.41 no.9
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• pp.678-683
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• 2008

The initial step during assembly of the hepatitis A virus particle is driven by domain 2A of P1-2A, which is the precursor of the structural proteins. The proteolytic removal of 2A from particulate VP1-2A by an as yet unknown host enzyme presumably terminates viral morphogenesis. Using a genetic approach, we show that a basic amino acid residue at the C-terminus of VP1 is required for efficient particle assembly and that host proteases trypsin and cathepsin L remove 2A from hepatitis A virus particles in vitro. Analyses of insertion mutants in the C-terminus of 2A reveal that this part of 2A is important for liberation of P1-2A from the polyprotein. The data provide the first evidence that the VP1/2A junction is involved in both viral particle assembly and maturation and, therefore, seems to coordinate the first and last steps in viral morphogenesis.

• Bulletin of the Korean Chemical Society
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• v.35 no.8
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• pp.2537-2540
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• 2014

• Molecules and Cells
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• v.39 no.9
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• pp.687-691
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• 2016

Transcription activator-like effector nucleases (TALENs) are powerful tools for targeted genome editing in diverse cell types and organisms. However, the highly identical TALE repeat sequences make it challenging to assemble TALEs using conventional cloning approaches, and multiple repeats in one plasmid are easily catalyzed for homologous recombination in bacteria. Although the methods for TALE assembly are constantly improving, these methods are not convenient because of laborious assembly steps or large module libraries, limiting their broad utility. To overcome the barrier of multiple assembly steps, we report a one-step system for the convenient and flexible assembly of a 180 TALE module library. This study is the first demonstration to ligate 9 mono-/dimer modules and one circular TALEN backbone vector in a one step process, generating 9.5 to 18.5 repeat sequences with an overall assembly rate higher than 50%. This system makes TALEN assembly much simpler than the conventional cloning of two DNA fragments because this strategy combines digestion and ligation into one step using circular vectors and different modules to avoid gel extraction. Therefore, this system provides a convenient tool for the application of TALEN-mediated genome editing in scientific studies and clinical trials.

• Proceedings of the Korean Vacuum Society Conference
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• 2011.08a
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• pp.204-204
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• 2011

During past decades, several types of peptide-based scaffolds, ranging from simple aromatic dipeptide to small protein fragments, have been studied to understand the underlying mechanism and mimic to create artificial nano/microstructures. However, a limited number of design principles have still been reported in peptidic scaffolds allowing well-defined self-assembled structure formation, presumably due to the intrinsic large conformational flexibility of natural peptides. In this presentation, we report the first example of highly homogeneous, well-defined and finite architectures by the ${\beta}$-peptide self-assembly.