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A KAIST research team developed in vivo flexible large scale integrated circuits
Daejeon, Republic of Korea, May 6th, 2013–-A team led by Professor Keon Jae Lee from the Department of Materials Science and Engineering at KAIST has developed in vivo silicon-based flexible large scale integrated circuits (LSI) for bio-medical wireless communication. Silicon-based semiconductors have played significant roles in signal processing, nerve stimulation, memory storage, and wireless communication in implantable electronics. However, the rigid and bulky LSI chips have limited uses in in vivo devices due to incongruent contact with the curvilinear surfaces of human organs. Especially, artificial retinas recently approved by the Food and Drug Administration (refer to the press release of FDA"s artificial retina approval) require extremely flexible and slim LSI to incorporate it within the cramped area of the human eye. Although several research teams have fabricated flexible integrated circuits (ICs, tens of interconnected transistors) on plastics, their inaccurate nano-scale alignment on plastics has restricted the demonstration of flexible nano-transistors and their large scale interconnection for in vivo LSI applications such as main process unit (MPU), high density memory and wireless communication. Professor Lee"s team previously demonstrated fully functional flexible memory using ultrathin silicon membranes (Nano Letters, Flexible Memristive Memory Array on Plastic Substrates), however, its integration level and transistor size (over micron scale) have limited functional applications for flexible consumer electronics. Professor Keon Jae Lee"s team fabricated radio frequency integrated circuits (RFICs) interconnected with thousand nano-transistors on silicon wafer by state-of-the-art CMOS process, and then they removed the entire bottom substrate except top 100 nm active circuit layer by wet chemical etching. The flexible RF switches for wireless communication were monolithically encapsulated with biocompatible liquid crystal polymers (LCPs) for in vivo bio-medical applications. Finally, they implanted the LCP encapsulated RFICs into live rats to demonstrate the stable operation of flexible devices under in vivo circumstances. Professor Lee said, "This work could provide an approach to flexible LSI for an ideal artificial retina system and other bio-medical devices. Moreover, the result represents an exciting technology with the strong potential to realize fully flexible consumer electronics such as application processor (AP) for mobile operating system, high-capacity memory, and wireless communication in the near future." This result was published in the May online issue of the American Chemical Society"s journal, ACS Nano (In vivo Flexible RFICs Monolithically Encapsulated with LCP). They are currently engaged in commercializing efforts of roll-to-roll printing of flexible LSI on large area plastic substrates. Movie at Youtube Link: Fabrication process for flexible LSI for flexible display, wearable computer and artificial retina for in vivo biomedical application http://www.youtube.com/watch?v=5PpbM7m2PPs&feature=youtu.be Applications of in Vivo Flexible Large Scale Integrated Circuits Top: In vivo flexible large scale integrated circuits (LSI); Bottom: Schematic of roll-to-roll printing of flexible LSI on large area plastics.
2013.06.09
View 13782
Neurotransmitter protein structure and operation principle identified
Professor Tae-Young Yoon - Real-time measurement of structural change of bio-membrane fusion protein - A new clue to degenerative brain diseases research KAIST Physics Department’s Professor Tae-Young Yoon has successfully identified the hidden structure and operation mechanism of the SNARE protein, which has a central role in transporting neurotransmitters between neurons, using magnetic nanotweezers. SNARE protein’s cell membrane fusion function is closely related to degenerative brain diseases or neurological disorders such as Alzheimer’s. Hence, this research may provide a clue to the disease’s prevention and treatment. Neurotransmission occurs when vesicles containing neurotransmitters fuse with cell membranes in neuron synapses. The SNARE protein is a cell-membrane fusion protein with a core role of releasing neurotransmitters. The academia speculated the SNARE protein would regulate the exchange of neurotransmitters, but its precise function and structure has been unknown. Professor Yoon’s research team developed an experimental technique using nanotweezers to measure physical changes to nanometer level by pulling and releasing each protein with force of 1 pN (piconewton). The research identified the existence of hidden SNARE protein"s intermediate structure. The process of withstanding and maintaining repulsive forces between bio-membranes in the hidden intermediate structure of SNARE to regulate the exchange of neurotransmitters has also been identified. Professor Yoon’s research team developed an experimental technique using magnetic nanotweezers to measure physical changes of proteins to nanometer level by pulling and releasing each protein with force of 1 pN. The research identified the existence of hidden SNARE protein"s intermediate structure and its formation. The process of withstanding and maintaining repulsive forces between bio-membranes in the hidden intermediate structure of SNARE to regulate the exchange of neurotransmitters has also been discovered. Professor Yoon said, “Ground breaking research results have been produced. A simple experimental technique of applying the smallest possible forces to proteins (with tweezers) to see their hidden structure and formation process can produce the same result as real observation has been developed.” He continued, “This technique will be very important in researching biological object with physical experimental technique. It will be a vital foundation to consilient research of different academia in the future.” This research was a joint project of Physics Department’s Professor Tae-Young Yoon, KAIST, and Biomedical Engineering Institute’s Professor Yeon-Kyun Shin at KIST. KAIST Physics Department’s Professor Yong-Hoon Cho, Ph.D. candidate Do-Yong Lee and KIAS Computational Sciences Department’s Professor Chang-Bong Hyun participated. The research was published on Nature Communications on April 16th. a) Neurotransmission occurs when vesicles containing neurotransmitters fuse with cell membranes in neuron synapses. A SNARE protein is a cell-membrane fusion protein with a core role of releasing neurotransmitters. b) A schematic diagram using magnetic nanotweezers to measure protein structure changes on molecular level. The nanotweezers exert an exquisite pull and release of each protein with a force of 1 pN to measure physical changes to nanometer level in real-time to observe the hidden intermediate structure and operation principles of bio-membrane fusion protein.
2013.05.25
View 9400
Complex responsible for protein breakdown in cells identified using Bio TEM
Professor Ho-Min Kim - High resolution 3D structure analysis success using Bio Transmission Electron Microscopy (TEM), a giant step towards new anticancer treatment development - Published in Nature on May 5th Using TEM to observe protein molecules and analysing its high resolution 3D structure is now possible. KAIST Biomedical Science and Engineering Department’s Professor Ho-Min Kim has identified the high resolution structure of proteasome complexes, which is responsible for protein breakdown in cells, using Bio TEM. This research has been published on the world"s most prestigious journal, Nature, online on May 5th. Our body controls many cellular processes through production and degradation of proteins to maintain homeostasis. A proteasome complex acts as a garbage disposal system and degrades cellular proteins when needed for regulation, which is one of the central roles of the body. However, a mutation in proteasome complex leads to diseases such as cancer, degenerative brain diseases, and autoimmune diseases. Currently, the anticancer drug Velcade is used to decrease proteasome function to treat Multiple Myeloma, a form of blood cancer. Research concerning proteasome complexes for more effective anticancer drugs and treatments with fewer side effects has been taking place for more than 20 years. There have been many difficulties in understanding proteasome function through 3D structure analysis since a proteasome complex, consisting of around 30 different proteins, has a great size and complexity. The research team used Bio TEM instead of conventionally used protein crystallography technique. The protein sample was inserted into Bio TEM, hundreds of photographs were taken from various angles, and then a high–performance computer was used to analyse its structure. Bio TEM requires a smaller sample and can analyse the complexes of great size of proteins. Professor Ho-Min Kim said, “Identifying proteasome complex assembly process and 3D structure will increase our understanding of cellular protein degradation process and hence assist in new drug development using this knowledge.” He added, “High resolution protein structure analysis using Bio TEM, used for the first time in Korea, will enable us to observe structure analysis of large protein complexes that were difficult to approach using protein crystallography.” Professor Kim continued, “If protein crystallography technology and Bio TEM could be used together to complement one another, it would bring a great synergetic effect to protein complex 3D structure analysis research in the future.” Professor Ho-Min Kim has conducted this research since his post-doctorate at the University of California, San Francisco, under the advice of Professor Yifan Cheng; in co-operation with Harvard University and Colorado University. Figure 1: A picture taken by Bio TEM of open state protein sample (proteasome complex) Figure 2: Bio TEM image analysis showing protein 3D structure
2013.05.25
View 11035
KAIST develops a low-power 60 GHz radio frequency chip for mobile devices
As the capacity of handheld devices increases to accommodate a greater number of functions, these devices have more memory, larger display screens, and the ability to play higher definition video files. If the users of mobile devices, including smartphones, tablet PCs, and notebooks, want to share or transfer data on one device with that of another device, a great deal of time and effort are needed. As a possible method for the speedy transmission of large data, researchers are studying the adoption of gigabits per second (Gbps) wireless communications operating over the 60 gigahertz (GHz) frequency band. Some commercial approaches have been introduced for full-HD video streaming from a fixed source to a display by using the 60 GHz band. But mobile applications have not been developed yet because the 60 GHz radio frequency (RF) circuit consumes hundreds of milliwatts (mW) of DC power. Professor Chul Soon Park from the Department of Electrical Engineering at the Korea Advanced Institute of Science and Technology (KAIST) and his research team recently developed a low-power version of the 60 GHz radio frequency integrated circuit (RFIC). Inside the circuit are an energy-efficient modulator performing amplification as well as modulation and a sensitivity-improved receiver employing a gain boosting demodulator. The research team said that their RFIC draws as little as 67 mW of power in the 60 GHz frequency band, consuming 31mW to send and 36mW to receive large volumes of data. RFIC is also small enough to be mounted on smartphones or notebooks, requiring only one chip (its width, length, and height are about 1 mm) and one antenna (4x5x1 mm3) for sending and receiving data with an integrated switch. Professor Park, Director of the Intelligent Radio Engineering Center at KAIST, gave an upbeat assessment of the potential of RFIC for future applications. What we have developed is a low-power 60-GHz RF chip with a transmission speed of 10.7 gigabits per second. In tests, we were able to stream uncompressed full-HD videos from a smartphone or notebook to a display without a cable connection (Youtube Link: http://www.youtube.com/watch?v=6PVSLBhMymc). Our chip can be installed on mobile devices or even on cameras so that the devices are virtually connected to other devices and able to exchange large data with each other."
2013.04.02
View 8734
New Structural Insight into Neurodegenerative Disease
A research team from the Korea Advanced Institute of Science and Technology (KAIST) released their results on the structure and molecular details of the neurodegenerative disease-associated protein Ataxin-1. Mutations in Ataxin-1 cause the neurological disease, Spinocerebella Ataxia Type 1 (SCA1), which is characterized by a loss of muscular coordination and balance (ataxia), as is seen in Parkinson’s, Alzheimer’s, and Huntington’s diseases. SCA1-causing mutations in the ATAXIN1 gene alter the length of a glutamine stretch in the Ataxin-1 protein. The research team provides the first structural insight into the complex formation of ATAXIN-1 with its binding partner, Capicua (CIC). The team, led by Professor Ji-Joon Song from the Department of Biological Sciences at KAIST, solved the structure of Ataxin-1 and CIC complex in atomic level revealing molecular details of the interaction between Ataxin-1 and CIC. Professor Song explained his recent research work, “We are able to see the intricate process of complex formation and reconfiguration of the two proteins when they interact with each other. Our work, we expect, will provide a new therapeutic target to modulate SCA1 neurodegenerative disease.” Understanding structural and molecular details of proteins at the atomic level will help researchers to track the molecular pathogenesis of the disease and, ultimately, design targeted therapies or treatments for patients, rather than just relieving the symptoms of diseases. Professor Song’s research paper, entitled “Structural Basis of Protein Complex Formation and Reconfiguration by Polyglutamine Disease Protein ATAXIN-1 and Capicua,” will be published in the March 15th issue of Genes & Development (www.genesdev.org). Complex Formation and Reconfiguration of ATAXIN-1 and Capicua The complex formation between a polyglutamine disease protein, ATXIN-1 and the transcriptional repressor Capicua (CIC) plays a critical role in SCA 1 pathogenesis. The image shows that the homodimerization of ATXIN-1 (yellow and red) is disrupted upon binding of CIC (blue). Furthermore, the binding of CIC to the ATXIN-1 induces a new form of ATXIN-1 dimerization mediated by CICs (ATXIN-1 AXH domains are shown in yellow and red, and CIC peptides shown in blue and white).
2013.04.02
View 9308
The new era of personalized cancer diagnosis and treatment
Professor Tae-Young Yoon - Succeeded in observing carcinogenic protein at the molecular level - “Paved the way to customized cancer treatment through accurate analysis of carcinogenic protein” The joint KAIST research team of Professor Tae Young Yoon of the Department of Physics and Professor Won Do Huh of the Department of Biological Sciences have developed the technology to monitor characteristics of carcinogenic protein in cancer tissue – for the first time in the world. The technology makes it possible to analyse the mechanism of cancer development through a small amount of carcinogenic protein from a cancer patient. Therefore, a personalised approach to diagnosis and treatment using the knowledge of the specific mechanism of cancer development in the patient may be possible in the future. Until recently, modern medicine could only speculate on the cause of cancer through statistics. Although developed countries, such as the United States, are known to use a large sequencing technology that analyses the patient’s DNA, identification of the interactions between proteins responsible for causing cancer remained an unanswered question for a long time in medicine. Firstly, Professor Yoon’s research team has developed a fluorescent microscope that can observe even a single molecule. Then, the “Immunoprecipitation method”, a technology to extract a specific protein exploiting the high affinity between antigens and antibodies was developed. Using this technology and the microscope, “Real-Time Single Molecule co-Immunoprecipitation Method” was created. In this way, the team succeeded in observing the interactions between carcinogenic and other proteins at a molecular level, in real time. To validate the developed technology, the team investigated Ras, a carcinogenic protein; its mutation statistically is known to cause around 30% of cancers. The experimental results confirmed that 30-50% of Ras protein was expressed in mouse tumour and human cancer cells. In normal cells, less than 5% of Ras protein was expressed. Thus, the experiment showed that unusual increase in activation of Ras protein induces cancer. The increase in the ratio of active Ras protein can be inferred from existing research data but the measurement of specific numerical data has never been done before. The team suggested a new molecular level diagnosis technique of identifying the progress of cancer in patients through measuring the percentage of activated carcinogenic protein in cancer tissue. Professor Yoon Tae-young said, “This newly developed technology does not require a separate procedure of protein expression or refining, hence the existing proteins in real biological tissues or cancer cells can be observed directly.” He also said, “Since carcinogenic protein can be analyzed accurately, it has opened up the path to customized cancer treatment in the future.” “Since the observation is possible on a molecular level, the technology confers the advantage that researchers can carry out various examinations on a small sample of the cancer patient.” He added, “The clinical trial will start in December 2012 and in a few years customized cancer diagnosis and treatment will be possible.” Meanwhile, the research has been published in Nature Communications (February 19). Many researchers from various fields have participated, regardless of the differences in their speciality, and successfully produced interdisciplinary research. Professor Tae Young Yoon of the Department of Physics and Professors Dae Sik Lim and Won Do Huh of Biological Sciences at KAIST, and Professor Chang Bong Hyun of Computational Science of KIAS contributed to developing the technique. Figure 1: Schematic diagram of observed interactions at the molecular level in real time using fluorescent microscope. The carcinogenic protein from a mouse tumour is fixed on the microchip, and its molecular characteristics are observed live. Figure 2: Molecular interaction data using a molecular level fluorescent microscope. A signal in the form of spike is shown when two proteins combine. This is monitored live using an Electron Multiplying Charge Coupled Device (EMCCD). It shows signal results in bright dots. An organism has an immune system as a defence mechanism to foreign intruders. The immune system is activated when unwanted pathogens or foreign protein are in the body. Antibodies form in recognition of the specific antigen to protect itself. Organisms evolved to form antibodies with high specificity to a certain antigen. Antibodies only react to its complementary antigens. The field of molecular biology uses the affinity between antigens and antibodies to extract specific proteins; a technology called immunoprecipitation. Even in a mixture of many proteins, the protein sought can be extracted using antibodies. Thus immunoprecipitation is widely used to detect pathogens or to extract specific proteins. Technology co-IP is a well-known example that uses immunoprecipitation. The research on interactions between proteins uses co-IP in general. The basis of fixing the antigen on the antibody to extract antigen protein is the same as immunoprecipitation. Then, researchers inject and observe its reaction with the partner protein to observe the interactions and precipitate the antibodies. If the reaction occurs, the partner protein will be found with the antibodies in the precipitations. If not, then the partner protein will not be found. This shows that the two proteins interact. However, the traditional co-IP can be used to infer the interactions between the two proteins although the information of the dynamics on how the reaction occurs is lost. To overcome these shortcomings, the Real-Time Single Molecule co-IP Method enables observation on individual protein level in real time. Therefore, the significance of the new technique is in making observation of interactions more direct and quantitative. Additional Figure 1: Comparison between Conventional co-IP and Real-Time Single Molecule co-IP
2013.04.01
View 18936
Ligand Recognition Mechanism of Protein Identified
Professor Hak-Sung Kim -“Solved the 50 year old mystery of how protein recognises and binds to ligands” - Exciting potential for understanding life phenomena and the further development of highly effective therapeutic agent development KAIST’s Biological Science Department’s Professor Hak-Sung Kim, working in collaboration with Professor Sung-Chul Hong of Department of Physics, Seoul National University, has identified the mechanism of how the protein recognizes and binds to ligands within the human body. The research findings were published in the online edition of Nature Chemical Biology (March 18), which is the most prestigious journal in the field of life science. Since the research identified the mechanism, of which protein recognises and binds to ligands, it will take an essential role in understanding complex life phenomenon by understanding regulatory function of protein. Also, ligand recognition of proteins is closely related to the cause of various diseases. Therefore the research team hopes to contribute to the development of highly effective treatments. Ligands, well-known examples include nucleic acid and proteins, form the structure of an organism or are essential constituents with special functions such as information signalling. In particular, the most important role of protein is recognising and binding to a particular ligand and hence regulating and maintaining life phenomena. The abnormal occurrence of an error in recognition of ligands may lead to various diseases. The research team focused on the repetition of change in protein structure from the most stable “open form” to a relatively unstable “partially closed form”. Professor Kim’s team analysed the change in protein structure when binding to a ligand on a molecular level in real time to explain the ligand recognition mechanism. The research findings showed that ligands prefer the most stable protein structure. The team was the first in the world to identify that ligands alter protein structure to the most stable, the lowest energy level, when it binds to the protein. In addition, the team found that ligands bind to unstable partially-closed forms to change protein structure. The existing models to explain ligand recognition mechanism of protein are “Induced Custom Model”, which involves change in protein structure in binding to ligands, and the “Structure Selection Model”, which argues that ligands select and recognise only the best protein structure out of many. The academic world considers that the team’s research findings have perfectly proved the models through experiments for the first time in the world. Professor Kim explained, “In the presence of ligands, there exists a phenomenon where the speed of altering protein structure is changed. This phenomenon is analysed on a molecular level to prove ligand recognition mechanism of protein for the first time”. He also said, “The 50-year old mystery, that existed only as a hypothesis on biology textbooks and was thought never to be solved, has been confirmed through experiments for the first time.” Figure 1: Proteins, with open and partially open form, recognising and binding to ligands. Figure 2: Ligands temporarily bind to a stable protein structure, open form, which changes into the most stable structure, closed form. In addition, binding to partially closed form also changes protein structure to closed form.
2013.04.01
View 11599
KAIST Develops Wireless Power Transfer Technology for High Capacity Transit
KAIST and the Korea Railroad Research Institute (KRRI) have developed a wireless power transfer technology that can be applied to high capacity transportation systems such as railways, harbor freight, and airport transportation and logistics. The technology supplies 60 kHz and 180 kW of power remotely to transport vehicles at a stable, constant rate. KAIST and KRRI successfully showcased the wireless power transfer technology to the public on February 13, 2013 by testing it on the railroad tracks at Osong Station in Korea. Originally, this technology was developed as part of an electric vehicle system introduced by KAIST in 2011 known as the On-line Electric Vehicle (OLEV). OLEV does not need to be parked at a charging station to have a fully powered battery. It gets charged while running, idling, and parking, enabling a reduction in size of the reserve battery down to one-fifth of the battery on board a regular electric car. The initial models of OLEV, a bus and a tram, receive 20 kHz and 100 kW power at an 85% transmission efficiency rate while maintaining a 20cm air gap between the underbody of vehicle and the road surface. OLEV complies with the national and international standards of 62.5 mG, a safety net for electromagnetic fields. In July 2013, for the first time since its development, OLEV will run on a regular road, an inner city route in the city of Gumi, requiring 40 minutes of driving each way. Today’s technology demonstration offers further support that OLEV can be utilized for large-scale systems. Professor Dong-Ho Cho, Director of Center for Wireless Power Transfer Technology Business Development at KAIST, explained the recent improvements to OLEV: “We have greatly improved the OLEV technology from the early development stage by increasing its power transmission density by more than three times. The size and weight of the power pickup modules have been reduced as well. We were able to cut down the production costs for major OLEV components, the power supply, and the pickup system, and in turn, OLEV is one step closer to being commercialized.” If trains receive power wirelessly, the costs of railway wear and tear will be dramatically reduced. There will be no power rails, including electrical poles, required for the establishment of a railway system, and accordingly, lesser space will be needed. Tunnels will be built on a smaller scale, lowering construction costs. In addition, it will be helpful to overcome major obstacles that discourage the construction of high speed railway systems such as noise levels and problems in connecting pantograph and power rails. KAIST and KRRI plan to apply the wireless power transfer technology to trams in May and high speed trains in September.
2013.03.19
View 12814
An efficient strategy for developing microbial cell factories by employing synthetic small regulatory RNAs
A new metabolic engineering tool that allows fine control of gene expression level by employing synthetic small regulatory RNAs was developed to efficiently construct microbial cell factories producing desired chemicals and materials Biotechnologists have been working hard to address the climate change and limited fossil resource issues through the development of sustainable processes for the production of chemicals, fuels and materials from renewable non-food biomass. One promising sustainable technology is the use of microbial cell factories for the efficient production of desired chemicals and materials. When microorganisms are isolated from nature, the performance in producing our desired product is rather poor. That is why metabolic engineering is performed to improve the metabolic and cellular characteristics to achieve enhanced production of desired product at high yield and productivity. Since the performance of microbial cell factory is very important in lowering the overall production cost of the bioprocess, many different strategies and tools have been developed for the metabolic engineering of microorganisms. One of the big challenges in metabolic engineering is to find the best platform organism and to find those genes to be engineered so as to maximize the production efficiency of the desired chemical. Even Escherichia coli, the most widely utilized simple microorganism, has thousands of genes, the expression of which is highly regulated and interconnected to finely control cellular and metabolic activities. Thus, the complexity of cellular genetic interactions is beyond our intuition and thus it is very difficult to find effective target genes to engineer. Together with gene amplification strategy, gene knockout strategy has been an essential tool in metabolic engineering to redirect the pathway fluxes toward our desired product formation. However, experiment to engineer many genes can be rather difficult due to the time and effort required; for example, gene deletion experiment can take a few weeks depending on the microorganisms. Furthermore, as certain genes are essential or play important roles for the survival of a microorganism, gene knockout experiments cannot be performed. Even worse, there are many different microbial strains one can employ. There are more than 50 different E. coli strains that metabolic engineer can consider to use. Since gene knockout experiment is hard-coded (that is, one should repeat the gene knockout experiments for each strain), the result cannot be easily transferred from one strain to another. A paper published in Nature Biotechnology online today addresses this issue and suggests a new strategy for identifying gene targets to be knocked out or knocked down through the use of synthetic small RNA. A Korean research team led by Distinguished Professor Sang Yup Lee at the Department of Chemical and Biomolecular Engineering, Korea Advanced Institute of Science and Technology (KAIST), a prestigeous science and engineering university in Korea reported that synthetic small RNA can be employed for finely controlling the expression levels of multiple genes at the translation level. Already well-known for their systems metabolic engineering strategies, Professor Lee’s team added one more strategy to efficiently develop microbial cell factories for the production of chemicals and materials. Gene expression works like this: the hard-coded blueprint (DNA) is transcribed into messenger RNA (mRNA), and the coding information in mRNA is read to produce protein by ribosomes. Conventional genetic engineering approaches have often targeted modification of the blueprint itself (DNA) to alter organism’s physiological characteristics. Again, engineering the blueprint itself takes much time and effort, and in addition, the results obtained cannot be transferred to another organism without repeating the whole set of experiments. This is why Professor Lee and his colleagues aimed at controlling the gene expression level at the translation stage through the use of synthetic small RNA. They created novel RNAs that can regulate the translation of multiple messenger RNAs (mRNA), and consequently varying the expression levels of multiple genes at the same time. Briefly, synthetic regulatory RNAs interrupt gene expression process from DNA to protein by destroying the messenger RNAs to different yet controllable extents. The advantages of taking this strategy of employing synthetic small regulatory RNAs include simple, easy and high-throughput identification of gene knockout or knockdown targets, fine control of gene expression levels, transferability to many different host strains, and possibility of identifying those gene targets that are essential. As proof-of-concept demonstration of the usefulness of this strategy, Professor Lee and his colleagues applied it to develop engineered E. coli strains capable of producing an aromatic amino acid tyrosine, which is used for stress symptom relief, food supplements, and precursor for many drugs. They examined a large number of genes in multiple E. coli strains, and developed a highly efficient tyrosine producer. Also, they were able to show that this strategy can be employed to an already metabolically engineered E. coli strain for further improvement by demonstrating the development of highly efficient producer of cadaverine, an important platform chemical for nylon in the chemical industry. This new strategy, being simple yet very powerful for systems metabolic engineering, is thus expected to facilitate the efficient development of microbial cell factories capable of producing chemicals, fuels and materials from renewable biomass. Source: Dokyun Na, Seung Min Yoo, Hannah Chung, Hyegwon Park, Jin Hwan Park, and Sang Yup Lee, “Metabolic engineering of Escherichia coli using synthetic small regulatory RNAs”, Nature Biotechnology, doi:10.1038/nbt.2461 (2013)
2013.03.19
View 10233
New Technology Will Enable the Commercialization of Plasmon Displays
-- Enhancements in the penetration ratios of color filters are expected by applying nano-surface plasmon effects. -- -- Color filter technology will be applicable to large-area OLED and LCD. -- The fabrication technology to commercialize display color filters using plasmon effects has been discovered. A joint research team headed by Professor Kyung Cheol Choi from the Department of Electrical Engineering of the Korea Advanced Institute for Science and Technology and Prof. Byeong-Kwon Ju from the School of Electrical Engineering of Korea University has developed the technology to design and produce a display color filter by applying nano-surface plasmon effects. Color filters are core components used to express colors in CMOS image sensors found in LCD/OLED displays or digital cameras. The current color filters have penetration ratios of 20~30%, but the objective of the joint research team is to raise this penetration ratio by over 40% to facilitate the mass production of energy-efficient plasmonic displays. Currently available plasmonic color filters are limited to applications on micrometer scales. However, outcomes of the newest research extend the size of the applications up to 2.5 cm by using laser interference lithography. The academic and industrial sectors agree that it is now possible to mass-produce displays using plasmonic color filters. The researchers built a nanohole array to large scale by using laser interference lithography, a technology that forms nanostructures with laser light interferences. They also suggested a new manufacturing process that can optimize the features of color filters while compensating for defects arising from the fabrication stages. The new manufacturing process of applying laser interference lithography is expected to overcome the shortcomings of traditional color filters by simplifying production and, enabling them to be produced at lower costs. “There were limitations to industrial applications of plasmon effect due to production costs, time, and yields,” explained Yun Seon Do, a Ph. D. candidate in the Department of Electrical Engineering of KAIST. “The new technology can reduce fabrication time and cost to the extent that it would be advisable to replace dye-based and pigment-based color filter technology." “This research can be applied to large-scale displays, such as TV screens, by using laser-interference lithography,” said Jung-Ho Park, a Ph. D. candidate in the School of Electrical Engineering of Korea University. “The research outcome is expected to be widely applied in advanced nano-manufacturing processes as it does not restrict the types of circuit boards." The research outcome, led by doctoral candidates Do and Park, appeared on the front cover of the second issue of Advanced Optical Materials, a highly regarded academic journal in the field of nanotechnologies, and the team has applied for six related patents.
2013.03.13
View 9089
Synthesis of a New Organic Supermolecule Succeeded
From left to right: Prof.Stoddart, Prof.Goddard and Prof.Jang Wook Choi KAIST EEWS graduate school’s research team led by Prof. Stoddart, Prof. Goddard and Prof. Jang Wook Choi has succeeded the synthesis of a new organic supermolecule that is stable in a radical condition under room temperature. Prof. Stoddart, who mainly led this research, is the world’s great scholar on orgaic molecular structure especially on catenane with an interconnection of several ring structures. Catenane is originated from Latin “catenane” referring to “chain”. The brief structure of the synthesized catenane is as following: Usually radicals are known to be unstable since they are electronically neutral and have very high reactivity. However, the radicals from this research showed air- and water- stability. It also showed a reversible change in oxidation number from o to +8 through chemical/electrochemical oxidation-reduction reaction. The phenomenon where paramagnetic and diamagnetic characteristics change according to the oxidation number has also been observed. Thus, the research like this - on the molecules showing various characteristics with stable radical - is expected to give a new direction to the next-generation electromemory system, semiconductor and energy storage system research. Meanwhile, this research, led by Prof.Stoddart team with Prof.Goddard and Prof. Jang Wook Choi’s team, is conducted under the support of Science and Technology’s World Class University project by Ministry of Education and published in ‘Science’ on 25th of Jan.
2013.02.24
View 11239
A Substance with Amazingly Improved Efficiency of Capturing Carbon Dioxides Developed
From left to right: Prof.Ali Coskun, Prof. Cafer T. Yavuz and Prof. Yousung Jung - Selectivity of CO2 increased by 300 times in comparison to nitrogen, published in Nature Communications- KAIST EEWS graduate school’s joint research team led by Prof. Cafer T. Yavuz, Prof. Ali Coskun, and Prof. Yousung Jung has developed the world"s most efficient CO2 absorbent that has 300 times higher carbon dioxide selectivity in comparison to nitrogen. Recently, the importance of CCS* technology, which is about capturing, storing and treating carbon dioxides, has begun to emerge world-widely as a practical alternative for the response to climate change. * CCS : Carbon Capture and sequestration Current carbon dioxide capturing technologies are wet capturing using liquid absorbent, dry capturing using solid absorbent and separation-membrane capturing using a thin membrane like a film. For the places like power plant and forge, where the emission of carbon dioxides is huge, the main task is to maintain the capturing efficiency under extremely hot and humid conditions. The previously studied dry absorbents, such as MOF or zeolite, had the disadvantages of instability in moist conditions and expensive cost for synthesis. On the other hand, the research team"s newly discovered dry absorbent, named ‘Azo-COP’, can be synthesized without any expensive catalysts so the production cost is very low. It is also stable under hot and humid conditions. COP is a structure consisting of simple organic molecules combined into porous polymer and is the first dry carbon dioxide capturing material developed by this research team. The research team introduced an additional functional group called "Azo" to the substance, so that it can selectively capture carbon dioxides among the mixture of gas. Azo-COP, which includes ‘Azo’ functional group, is manufactured easily by using common synthesis methods, and impurities are removed simply by using cheap solvents like water and acetone instead of expensive catalysts. As a result, the manufacturing cost has lowered drastically. Especially, Azo-COP is combined with carbon dioxides by weak attraction force rather than chemical attraction so the recycling energy cost for the absorbent can be reduced innovatively, and it is expected to be used for capturing substances other than carbon dioxides in various areas as it is stable under extreme conditions even under 350 degrees Celsius. This research is supported by Korea Carbon Capture&Sequestration R&D Center(Head: Sangdo Park) and KAIST EEWS planning group. Prof. Cafer T. Yavuz and Prof. Ali Coskun said that “when Azo-COP is used for separation of CO2 and N2, the capturing efficiency has increased by hundred times.” He continued “This substance does not need any catalysts and has great chemical characteristics like water stability and structure stability so is expected to be used in various fields including carbon dioxides capturing” Meanwhile, this research is published in ‘Nature’s stablemate ‘Nature Communications’ on 15th of Jan.
2013.02.24
View 12410
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