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Professor Jay H. Lee to receive the 2013 AIChE CAST Computing in Chemical Engineering Award
Professor Jay H. Lee of Chemical and Biomolecular Engineering Department at KAIST has won the 2013 Computing in Chemical Engineering Award of AIChE"s CAST Division (AIChE, American Institute of Chemical Engineers and CAST, Computing & Systems Technology Division).
The CAST Computing in Chemical Engineering Award, sponsored by The Dow Chemical Company, is annually given to an individual who has made outstanding contributions in the application of computing and systems technology to chemical engineering.Professor Lee has been recognized for his pioneering research contributions for “novel paradigms for much improved and robust model predictive control in industrial processes.” He is currently the Head of Chemical and Biomolecular Engineering Department and Director of Brain Korea (BK) 21 Program at the department. BK21 is the Korean government’s initiative to support the growth of research universities in the nation and foster highly trained master’s and doctoral students as well as researchers.
The CAST Computing in Chemical Engineering Award will be presented to Professor Jay H. Lee at the CAST Division dinner to be held at the AIChE Annual Meeting this November in San Francisco, where he will also deliver the after dinner lecture associated with this award.
2013.06.12 View 9408 -
KAIST Department of Mechanical Engineering Ranked in 19th Place
- Ranked in 19th place in 2013 Quacquarelli Symonds (QS) World University Rankings by Engineering, Mechanical, Aeronautical and Manufacturing Subjects -
KAIST ranked 19th in 2013 QS World University Rankings by Subject in Engineering, Mechanical, Aeronautical and Manufacturing Subjects. This is great progress compared to last year’s 51st-100th rank.
The 2013 QS World University Rankings used four indicators, including academic reputation, employer reputation, citations per paper, and H-index citations, to assess 2,858 universities in the world, and evaluated up to 200th place in 30 academic subjects.
KAIST earned high remarks from the H-index citations indicator, which is a new criteria introduced in the employer reputation rating. Moreover, the employer reputation section has risen sharply compared to the previous year. The H-index measures qualitatively and quantitatively the research outcomes of the researchers and assesses the number of papers written per professor and the average citation frequency of the papers.
The proportions of the indicators differ by subjects. For the mechanical engineering field, they weigh 40%, 30%, 15%, and 15%, respectively.
Rank
Academic
Employer
Citations per paper
H-index Citations
Score
19 (51-100)
68.1 (78.9)
89.1 (60.2)
84.6 (83.1)
93.1 (N/A)
80.4 (74.6)
2013.06.10 View 7132 -
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 12423 -
International Student Conference (ICISTS-KAIST) to be Held in August
- 300 participants including university students worldwide and renowned speakers expected to gather
- Ideal coexistence of science & technology and society explored under the theme of “Perfect Alliance”
Science & technology and society are at the core of 21st century’s development. ICISTS-KAIST 2013, international conference for university students, seeks ways for the two to coexist harmoniously and is to be held from August 5 to 9 on KAIST campus as well as at Daejeon Convention Center.
ICISTS stands for International Conference for the Integration of Science, Technology and Society. ICISTS-KAIST is a non-profit organization run by KAIST students who are directly engaged in the coordination, planning, finance, public relations, and management of this academic event. The upcoming ninth annual event of ICISTS (www.icists.org) 2013 is centered around the theme, “Perfect Alliance: Coexistence for Human Society.” The conference will last for four nights and five days; scholars and students across various academic backgrounds gather to narrow the gap between fields of study and discuss possible solutions to the problems in today’s society.
The annual conference, ICISTS-KAIST attracts hundreds of participants from all over the world to KAIST, Daejeon and its most recent event last year witnessed discussions among some 300 students from 22 countries hearing the lectures from 40 academics and scholars. This year’s event will welcome the 16-year old inventor, scientist, and cancer researcher Jack Thomas Andraka, the founder of the “One Laptop Per Child” project Walter Bender, Chemistry Nobel Prize laureate Harold Walter Kroto, and many more.
The application period for ICISTS-KAIST 2013 runs from May 20 to July 12, and applications are received through the website at www.icists.org.
ICISTS-KAIST 2013 Promgram Summary
Event Title: International Conference for the Integration of Science, Technology and Society 2013 (ICISTS-KAIST 2013)
Theme: Perfect Alliance: Coexistence for Human Society
Date and Venue: 2013 Aug. 5 (Mon.) ~ Aug. 9 (Fri.), KAIST Campus and Daejeon Convention Center
Host and Organizer: ICISTS KAIST
Sponsor: Korean National Commission for UNESCO, Korea Tourism Organization, Korea Ministry of Education, Science & Technology, KOFST
Session Description:
Keynote Speech - Keynote address on fundamental approach to coexistence
Parallel Session - Multiple simultaneous lecture of delegates’ choice
Group Discussion - Small group discussions among delegates and speakers
Panel Discussion - In-depth and thought-revealing discussion among speakers
Experience Session - First-person experience on relevant technology
Team Project & Poster Fair - Team mission, poster exhibition and evaluation
Subtopics:
- New Values from Coexistence of Science & Technology and Society
- Synergetic Resolution via Coexistence of Science & Technology and Society
- Essential Communication for Coexistence of Science & Technology and Society
Notable Speakers:
- Gretchen Kalonji: Assistant to Director-General at UNESCO
- Sheila Jasanoff: Director of STS Program at Harvard Kennedy School
- Walter Bender: Former Director of MIT Media Lab and One Laptop Per Child- Jack Andraka: 16-year old Cancer Resesarcher
2013.05.31 View 8475 -
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 8626 -
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 9980 -
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 17208 -
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 10382 -
Launched the Saudi Aramco-KAIST CO2 Management Center in Korea
KAIST and Saudi Aramco, a global energy and petrochemicals enterprise, signed on February 20, 2013 the Master Research and Collaboration Agreement (the Agreement) on joint collaborations in research and development of carbon management between the two entities.
The Agreement was subsequently concluded upon the signing of the Memorandum of Understanding (MOU) between KAIST and Saudi Aramco, dated January 7th, 2013. In the Agreement, the two organizations specified terms and conditions necessary to conduct joint research projects and stipulated governing body for the operation of the Saudi Aramco-KAIST CO2 Management Center.
KAIST and Saudi Aramco, a national oil company for Saudi Arabia, entered into the MOU, in which the two parties shared a common interest in addressing the issue of CO2 capture, CO2storage, CO2 avoidance using efficiency improvements, and converting CO2 into useful chemicals and other materials, and agreed to “create a major research center for CO2” in Korea.
As envisioned by the MOU and its subsequent agreement, KAIST and Saudi Aramco decided to operate an interim office of the Saudi Aramco-KAIST CO2 Management Center at KAIST campus in Daejeon, Korea, pending the establishment of the research center. The full-fledged, independent research facility will be built at a location and during a period to be agreed between the two parties.
Following the signing of the Agreement, there was a celebration event taken place, including a signboard hanging ceremony for the interim research office. A 10-member delegation from Saudi Aramco, which was headed by Vice President of Engineering Services Samir Al-Tubayyeb, Dr. Nam-Pyo Suh, former president of KAIST, Vice President of Research at KAIST Kyung-Wook Paik, and senior representatives from Korean oil and petrochemical companies such as S-Oil, Lotte Chemicals, SK Innovation, and STX attended the event.
Kyung-Wook Paik, Vice President of Research at KAIST, said,
“In order to help find solutions to carbon management, KAIST and Saudi Aramco will facilitate to exchange each party’s complementary technical expertise, gain insight into new research fields, and have access to key sources of talent, while promoting innovation for technology solutions and contributing to the lifelong learning agenda of both organizations.”
Samir Al-Tubayyeb, Vice President of Engineering Services at Saudi Aramco, added that “As a world-leading oil and gas company, Saudi Aramco’s mission is to promote the continued use of safe, environmentally-friendly petroleum products with a vision to becoming a global leader in research and technology. Building a strong and cooperative relationship with KAIST in our endeavor to search for alternative ways to better utilization of fossil fuels will expedite the creation of opportunities to make the world environmentally safer and sustainable.”
KAIST and Saudi Aramco will each chip in a maximum of USD 5 million annually for the establishment and operation of the Saudi Aramco-KAIST CO2 Management Center during the initial term of the Master Research and Collaboration Agreement, which starts in 2013 and continues through 2018.
2013.03.19 View 13060 -
KAIST Inaugurates Its 15th President
President Sung-Mo “Steve” Kang praised what KAIST has achieved as a powerful engine for the economic and industrial advancement of Korea over the past 41 years, while pledging to continue its endeavor “to go above and beyond its present accomplishments.”
KAIST inaugurated its 15th president, Sung-Mo “Steve” Kang, on February 27, 2013, in a ceremony at the auditorium of its main campus in Daejeon, South Korea. President Kang delivered his inauguration speech to 1,000 distinguished guests from government and public offices and the nation’s science community, including Chairman Myung Oh of the KAIST Board of Trustees, Former Presidents of KAIST Soon-Dal Choi and Chang-Sun Hong, Former National Assembly Member Yong-Kyung Lee, and members of the university.
In his speech, President Kang recalled that he had formed a strong bond with KAIST over many years, before assuming the presidency and extolled the university’s contribution to Korea’s current economic prowess. Referring to the “growing pains” that KAIST has experienced amid its successes, he vowed to unify the university community to take another leap forward:
We must ease the pain through trust and consideration for one another and join in unity to take steps toward the brighter tomorrow of KAIST. I humbly seek your help and pledge to put forth my utmost effort as a servant and leader.
Speaking of KAIST’s importance to the Korean nation, President Kang said, “Korea, as a nation lacking a deep pool of natural resources, must find innovative ways to compete globally to ensure the prosperity and well-being of its people.” He emphasized KAIST’s role as a catalyst to “lead the nation toward the frontiers of science and technology with fervor and responsibility.”
In order to become a global leader in higher learning and contribute to the advancement of science and technology in Korea and beyond, President Kang said that KAIST must do well in five areas with letters matching those of its own acronym: Knowledge creation, Advancement on all fronts, Integrity, Sustainability, and Trust.
In knowledge creation, the president pointed out the necessity of collaboration, student-centered and faculty-led research programs, and interdisciplinary research. For advancement on all fronts, he proposed redrafting KAIST’s future blueprint by consulting with all of its constituents and the Board of Trustees to improve the overall efficiency of the university.
President Kang added that KAIST should uphold integrity in all research publications, financial management, and human relations to withstand unforeseen challenges and problems and that is should seek sustainable value for education and research, not becoming overly driven by short-term research goals. Last, he said that KAIST must be an institution trusted by the public and KAIST faculty, students, and staff. This culture of trust can be made possible, he added, when the members of the university do their best to create an environment of understanding and caring for each other.
President Kang concluded his remarks by promising that he would always open his door and welcome anyone for visits, discussions, and sharing. Known as “Captain Smooth” for the well-rounded, warm, yet decisive leadership style that he showed during his chancellorship at the University of California, Merced, President Kang now pledges to guide KAIST to become better and stronger in the next four years. For a full transcript of the speech, download the PDF file below.
2013.03.13 View 7465 -
President Sung-Mo 'Steve' Kang Welcomed the Class of 2017
KAIST held its 2013 Opening Convocation on Monday, March 4, 2013, on its campus in Daejeon, South Korea, with 717 newly arrived freshmen and their parents, family, and friends.
In his welcoming speech, President Sung-Mo “Steve” Kang congratulated the students on their admission to KAIST after a rigorous selection process. President Kang advised the freshmen to follow four principles for successful college lives: development of good character and integrity, acquisition of diverse knowledge and experiences, global awareness, and establishment of fellowship and friendship. For a full transcript of the speech, download the PDF file below.
2013.03.13 View 6150 -
Op-Ed by Professor David Helfman: Global Science and Education in Korea for the 21st Century
Professor David Helfman from the Department of Biological Sciences and Graduate School of Nanoscience and Technology contributed an op-ed, “Global Science and Education in Korea for the 21st Century, to the Korea Herald on February 20, 2013. For the article, please click the link below:
http://www.koreaherald.com/view.php?ud=20130220000623.
2013.02.26 View 9410