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Cooperation Agreement signed between KAIST and University of Oxford
On April 6th, a Cooperation Memorandum of Understanding (MOU), including the exchange of students between two universities, was signed by KAIST and University of Oxford on April 6th.
In the MOU, KAIST and Oxford agreed to achieve mutual development through cooperation, such as joint research programs and the exchange of professors and students.
President Sung-Mo Kang stated, “This agreement will be the start of close cooperation between the two universities, and I will continue to endeavor to expand the relationship.”
Andrew Hamilton, the president of Oxford University replied, “I am well aware of the excellent quality of teaching and research of Korean students and KAIST. I hope the cooperation between KAIST and Oxford will achieve exchange at diverse levels.”
President Hamilton taught chemistry at the University of Pittsburgh and Princeton University and also served as the vice-president of Yale University. Having experience of teaching a KAIST student before, he has high praise for the ability of KAIST students.
The President of the University of Oxford, Andrew Hamilton (left), and the President of KAIST, Sung-Mo "Steve" Kang, shake hands in acknowledgement of signing the Cooperation MOU.
2013.05.20 View 6598 -
KAIST signs a Cooperation Agreement with University of California, Irvine
On April 6th, KAIST signed a cooperation memorandum of understanding (MOU) establishing academic exchanges of faculty and students with the University of California, Irvine (UC Irvine).
The MOU states that the collaboration between both universities will promote the exchange of faculty and students, as well as joint research.
Following UC Los Angeles (UCLA), Irvine became the second UC campus to make the exchange agreement with KAIST.
UC Irvine was founded in 1965, and is known as a prestigious public university composed of 13 departments, including colleges of arts, biological sciences, engineering, and humanities.
The ceremony was attended by KAIST President, Sung-Mo Kang, and UC Irvine President, Michael V. Drake, as well as Suk-Hee Kang, the former Mayor of Irvine.
KAIST President Sung-Mo "Steve" Kang (left) and President of UC Irvine Michael Drake (right) shake hands after signing the Cooperation MOU.
2013.05.20 View 6377 -
KAIST Holds Robot Taekwondo Competition Recognized by the World Taekwondo Federation
KAIST will host the 12th Intelligent System-on-Chip (SoC) Robot War in October 2013, a robot competition. The event will have two entries: robot Taekwondo contest and HURO competition.
The World Taekwondo Federation has decided to offer an honorary Taekwondo degree to the winner of SoC Taekwondo Robot competition.
The Intelligent SoC Robot War was created in 2002 by KAIST’s Professor Hoi-Jun Yoo in the Department of Electrical Engineering.
For SoC Taekwondo Robot event, two robots compete in the form of Taekwondo, traditional Korean martial arts. The robots competing in this event have a camera and semiconductor chips on board, and therefore they have the brain-like functions to identify an object and control movements on their own. The robots have 21 joints with humanoid robot technology on their body for the techniques needed to compete in a typical Taekwondo match. They employ moves such as front kicks, side kicks, and upper punches.
In particular, KAIST’s System Design Innovation & Application Research Center, the organizer of this competition, has operated a team to demonstrate robot Taekwondo since last year with the purpose of displaying the basic movements of Taekwondo.
“Robots received attention as the source of growth in the near future. We have been developing robotics technology, and as part of our endeavor, preparing the Taekwondo demonstration team since 2012 to exhibit Korea’s robot technology and introduce our traditional martial arts,” said Professor Hoi-Jun Yoo. “We will continue to develop various capabilities for Taekwondo robots in cooperation with the World Taekwondo Federation.”
In HURO-Competition, robots compete for crossing the finishing line first by completing various missions, such as putting in a golf ball or overcoming obstacles while avoiding unexpected accidents. The winning team is awarded with a Presidential Award of Korea.
The 12th Intelligent SoC Robot War Competition is open to all graduate or undergraduate students. For details, visit the homepage at http://www.socrobotwar.org/.
2013.05.06 View 9970 -
KAIST hosts 2013 Wearable Computer Contest
2013 Wearable Computer Contest (WCC) will be held in early November. This year’s contest is hosted by KAIST and sponsored by Samsung Electronics.
Wearable computers are drawing attention in the IT world as a potentially convenient information and communication device for future generations, which are attached to clothing or on the body. As smartphones have grown increasingly more popular, various supporting devices are being developed. The IT industry is targeting wearable computers for future development. The main leaders of the field, Samsung, Apple (i-Watch) and Google (Google Glasses) are joining the race for its development.
European and US firms halted their research in wearable computers in the 2000s, but there has been a great burst of interest recently. Korea has been consistently taking on wearable computer research since 2003 and held the Wearable Computer Contest for the last nine years. Since 2005, the contest aims to promote leading edge technological research and Intellectual Property (IP) as well as cultivate a professional workforce in Korea. The contest has promoted world class research in the field of wearable computer technology.
Moreover, KAIST has increased support for its competing teams through Samsung sponsorship and is considering applying the technology from the contest into Samsung products. Winning teams receive 1,500,000 Korean won and Samsung smart IT devices to produce an actual wearable computer. KAIST has increased the number of members who can participate in the competing teams in the finals from 10 to 15 to provide more opportunities to develop wearable computers.
With the theme “Smart IT: Any-information for Anybody,” the 2013 Wearable Computer Contest requires competing teams to suggest an innovative idea which combines IT and fashion for wearable computers. Teams that pass the paper and presentation evaluation go on to the finals, where 15 teams will have four months of production period for the final evaluation in November.
The final teams also receive systematic education on ubiquitous computing, wearable computer platforms, and Human-Computer Interaction (HCI).
The Wearable Computer Contest is holding an ideas contest pitched in a poster format. This contest evaluates proposals for wearable computers, and there is no requirement to enter the rest of the contest. Anyone can compete without having to physically make the product.
More information on the registration and the contest can be found at http://www.ufcom.org/.
2013.04.30 View 7264 -
Professor Sang-Ouk Kim Interviewed with Arirang TV on April 15, 2013
Professor Sang-Ouk Kim from the Department of Materials Science and Engineering made an appearance on April 15, 2013 at a morning show called “Korea Today” on Arirang TV, an English-language network based in Seoul, South Korea.
Professor Kim introduced his research on the development of flexible semiconductor technology. If commercialized, Professor Kim added, the technology would expedite the common use of wearable computers including mobile devices as well as the development of bio-medical implanted and wireless telemetry bio-devices. To play the video, please click the link below (00:25:00): http://www.arirang.co.kr/Player/TV_Vod.asp?HL=X&code=VOD&vSeq=68872
2013.04.30 View 8469 -
Distinguished Professor Sang-Yup Lee received 2013 Amgen Biochemical Engineering Award
- Previous award winners are world-renowned scholars of biochemical engineering including James Bailey, Michael Shuler and Daniel Wang
KAIST Chemical and Biomolecular Engineering Department’s Professor Sang-Yup Lee has been selected to receive the 2013 Amgen Biochemical Engineering Award. The award ceremony will take place this June at the International Biochemical and Molecular Engineering conference in Beijing, China.
The Amgen Biochemical Engineering Award was established by Amgen, a world renowned American pharmaceutical company, in 1993. Amgen awards leading biochemical engineers every two years. The first Amgen award recipient was James Bailey of the California Institute of Technology (Caltech) in 1993. Since then leading engineers that are sometimes called “founding fathers of biochemical engineering” have received the award including MIT Professor Daniel Wang and Michael Shuler of Cornell University.
The first nine award winners were Americans and in 2011 Jens Nielson of Chalmers University of Technology, Sweden, received the Amgen award as a non-American. Professor Sang-Yup Lee is the first Asian to receive the award.
The Amgen award panel said, “Professor Lee made an incredible contribution to the fields of synthetic biology and industrial bioengineering by finding chemical material, fuel, protein and drug production and system bioengineering through metabolic engineering of microorganisms.”
Professor Lee is an expert in metabolic engineering of microorganisms and contributed to the development of system metabolic engineering and system bioengineering. Furthermore, he developed various medical and chemical products and processes which were then applied to synthesise strains of succinate, plastics, butanol and nylon.
Professor Lee is a fellow of the Korean Academy of Science and Technology and National Academy Engineering of Korea; an international member of National Academy of Engineering (US); a former fellow of the American Association for the Advancement of Science; a member of the American Institute of Chemical Engineers, the American Industrial Microbiology Society and American Academy of Microbiology. He is currently Head of Global Agenda Council on Biotechnology and is world renowned for his work in biotechnology field.
2013.04.30 View 8169 -
Popular Science May 2013: Online Electric Vehicle (OLEV) Introduced as Part of Smart Roads
Popular Science (PopSci), a famous American monthly magazine publishing popular science articles for general readers on science and technology subjects, introduced KAIST’s Online Electric Vehicle (OLEV) in its latest issue of May 2013. For the article, please see the attachment.
2013.04.25 View 7098 -
Award Winning Portable Sound Camera Design
- A member of KAIST’s faculty has won the “Red Dot Design Award,” one of three of the most prestigious design competitions in the world, for the portable sound camera.
KAIST’s Industrial Design Professor Suk-Hyung Bae’s portable sound camera design, made by SM Instruments and Hyundai, has received a “Red Dot Design Award: Product Design,” one of the most prestigious design competitions in the world.
If you are a driver, you must have experienced unexplained noises in your car. Most industrial products, including cars, may produce abnormal noises caused by an error in design or worn-out machinery. However, it is difficult to identify the exact location of the sound with ears alone.
This is where the sound camera comes in. Just as thermal detector cameras show the distribution of temperature, sound cameras use a microphone arrangement to express the distribution of sound and to find the location of the sound. However, existing sound cameras are not only too big and heavy, their assembly and installation are complex and must be fixed on a tripod. These limitations made it impossible to measure noises from small areas or the base of cars.
The newly developed product is an all-in-one system resolving the inconvenience of assembling the microphone before taking measurements. Moreover, the handle in the middle is ergonomically designed so users can balance its weight with one hand. The two handles on the sides work as a support and enable the user to hold the camera in various ways.
At the award ceremony, Professor Suk-Hyung Bae commented, “The effective combination of cutting edge technology and design components has been recognized.” He also said, “It shows the competency of the KAIST’s Department of Industrial Design, which has a high understanding of science and technology.”
On the other hand, SM Instruments is a sound vibration specialist company which got its start from KAIST’s Technology Business Incubation Centre in 2006 and earned its independence by gaining proprietary technology in only two years. SM Instruments is contributing to developing national sound and vibration technology through relentless change and innovation. ;
Figure 1: Red Dot Design Award winning the portable sound camera, SeeSV-S205
Figure 2: Identifying the location of the noise using the portable sound camera
Figure 3: The image showing the sound distribution using the portable sound camera
2013.04.09 View 19012 -
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 8118
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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 8532 -
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 17185 -
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 10371