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Technology Developed to Control Light Scattering Using Holography
Published on May 29th Nature Scientific Reports online
Recently, a popular article demonstrated that an opaque glass becomes transparent as transparent tape is applied to the glass. The scientific principle is that light is less scattered as the rough surface of the opaque glass is filled by transparent tape, thereby making things behind the opaque glass look clearer.
Professor Yong-Keun Park from KAIST’s Department of Physics, in a joint research with MIT Spectroscopy Lab, has developed a technology to easily control light scattering using holography. Their results are published on Nature’s Scientific Reports May 29th online edition.
This technology allows us to see things behind visual obstructions such as cloud and smoke, or even human skin that is highly scattering, optically thick materials. The research team applied the holography technology that records both the direction and intensity of light, and controlled light scattering of obstacles lied between an observer and a target image. The team was able to retrieve the original image by recording the information of scattered light and reflecting the light precisely to the other side.This phenomenon is known as “phase conjugation” in physics. Professor Park’s team applied phase conjugation and digital holography to observe two-dimensional image behind a highly scattering wall. “This technology will be utilized in many fields of physics, optics, nanotechnology, medical science, and even military science,” said Professor Park. “This is different from what is commonly known as penetrating camera or invisible clothes.” He nevertheless drew the line at over-interpreting the technology, “Currently, the significance is on the development of the technology itself that allows us to accurately control the scattering of light."
Figure I. Observed Images
Figure II. Light Scattering Control
2013.07.19 View 8823 -
Joint Research Center on EEWS with Hyundai Heavy Industries Plans to Open
The research center will conduct collaborative R&D projects on energy, environment, water, and sustainability for the next five years.Hyundai Heavy Industries (HHI), the world’s largest shipbuilding company, signed an MOU with KAIST for future business development and joint research collaboration.
KAIST and HHI signed an MOU as an agreement to establish the “HHI-KAIST EEWS Research Center (HK Research Center) on June 21st.”
The major mission of the HK Research Center is to build a strong base for creating future businesses through developing fundamental, core technology in the field of EEWS and designing business models based on the new technology.
Toward this goal, HHI will sponsor the R&D budget and operation expenses of the research center for the next five years.
Prior to the signing of the MOU, a delegation from HHI, led by the Vice President, Mr. Si-Young Hwang, visited the Office of EEWS Initiative at KAIST and held a workshop. During the workshop, HHI and KAIST agreed to collaborate in fields such as LNG-propelled ships, solar power generation, energy storage, fuel cells, and CO2 capture.
KAIST has run a EEWS graduate program that receives government grants over the last five years, with a research emphasis on energy, environment, water, and sustainability, which are crucial issues to humankind in the 21st century. The EEWS program achieved 24 core technological developments and educates more than 200 masters- and PhD-degree students annually.
The EEWS program also emphasizes commercializing its research outcomes. Through the annual Business Planning Competition and Investment Drive, there have been eight new companies founded by alumni and professors over the last five years of the program. The HK Research Center will be an excellent foundation for future education and research in EEWS.
Professor Jae-Kyu Lee, the head of the HK Research Center and the director of the EEWS Initiative, said, “This event is a benchmarking example of Industry-KAIST collaboration. We hope that the HK Research Center will be a place for disruptive innovations to translate into creative business opportunities.”
MOU signed for Hyundai Heavy Industries-KAIST EEWS Research Center
2013.07.15 View 8869 -
Chin-Wan Chung, a professor of computer science, received the best paper award from ACM
The Korea Times reported on July 12, 2013 that Chin-Wan Chung, a professor of computer science at KAIST, won the best paper award by the Association for Computing Machinery (ACM). For the article, please click the link:
http://koreatimes.co.kr/www/news/people/2013/07/178_139132.html
2013.07.15 View 7348 -
Prof. Song Chong received the IEEE William R. Bennett Prize Paper Award
The IEEE (Institute of Electrical and Electronics Engineers) Communications Society (ComSoc), a renowned global network of professionals with a common interest in advancing communications technologies, has announced the winner of the 2013 William R. Bennett Prize in the field of communications networking. The prize was given to a Korean research team led by Song Chong, Professor of Electrical Engineering at KAIST and Injong Rhee, Professor of Computer Science at North Carolina State University. In addition, Dr. Minsu Shin, Dr. Seongik Hong, and Dr. Seong Joon Kim of Samsung Electronics Co., Ltd. as well as Professor Kyunghan Lee from Ulsan National Institute of Science and Technology were recognized for their contribution.
The William R. Bennett Prize for communications networking has been awarded each year since 1994 in recognition of the best paper published in any journal financially sponsored or co-sponsored by ComSoc in the previous three calendar years. Only one paper per year is selected based on its quality, originality, scientific citation index, and peer reviews. Among the previous award winners are Robert Gallager of MIT, and Steven Low of the California Institute of Technology, and Kang G. Shin of the University of Michigan.
The Korean research team’s paper, On the Levy-Walk Nature of Human Mobility, was published in the June 2011 issue of IEEE/ACM Transactions on Networking, a bimonthly journal co-sponsored by the IEEE ComSoc, the IEEE Computer Society, and the Association for Computing Machinery (ACM) with its Special Interest Group on Data Communications (SIGCOMM).
In the paper, the research team proposed a new statistical model to effectively analyze the pattern of individual human mobility in daily life. The team handed out GPS (global positioning system) devices to 100 participants residing in five different university campuses in Korea and the US and collected data on their movements for 226 days. The mobility pattern obtained from the experiment predicted accurately how the participants actually moved around during their routines. Since publication, the paper has been cited by other papers approximately 350 times.
The team’s research results will apply to many fields such as the prevention and control of epidemics, the design of efficient communications networks, and the development of urban and transportation system.
The research team received the award on June 10th at the 2013 IEEE International Conference on Communications (ICC) held in Budapest, Hungary, from June 9-13, 2013.
Professor Song Chong
2013.07.06 View 13748 -
Thinking Out of the Box: KAIST Silicon Valley Innovation Platform
KAIST established a liaison office in San Jose, California, to support the entrepreneurship of KAIST graduates, students, and faculty who aspire to transform their innovative ideas into business.
The office, KAIST Silicon Valley Innovation Platform (SVIP), is located within the Korea Trade-Investment Promotion Agency (KOTRA) IT Center on North First Street in San Jose.
SVIP collects information and analyzes trends on emerging technologies; provides various educational programs on entrepreneurship and technology translation; offers opportunities to prospective entrepreneurs to engage with industry and research and government organizations; and assists Korean startups in accessing the US and North American market.
President Steve Kang attended the opening ceremony of the office on June 14th and encouraged KAIST alumni living in the US to share their ideas and technology innovations and transform them into business opportunities.
For more information, please contact Professor Soung-Hie Kim (seekim@business.kaist.ac.kr) from the Graduate School of Information and Media Management, KAIST.
2013.07.04 View 8856 -
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 10508 -
Technology for Non-Breaking Smartphone Display Developed
High-strength plastic display has been developed by applying a glass-fiber fabric.
“Will bring about innovation to the field by replacing glass substrates”
It is now possible to manufacture non-breaking smartphone display. Heavy glass substrates of large-screen televisions will be replaced with light plastic films.
Professor Choon Sup Yoon from KAIST’s Department of Physics and KAIST Institute for Information Technology Convergence has developed the technology for high-strength plastic substrates to replace glass displays.
The plastic substrate created by Professor Yoon and his research team have greatly enhanced needed properties of heat resistance, transparency, flexibility, inner chemical capability, and tensile strength. Although the material retains flexibility as a native advantage of plastic film, its tensile strength is three times greater than that of normal glass, which is a degree similar to tempered glass. In addition, Professor Yoon’s substrate is as colorless and transparent as glass and resists heat up to 450℃, while its thermal expansivity is only 10% to 20% of existing plastics.
Glass substrates are currently used in practically every display such as mobile phone screens, televisions, and computer monitors for having smooth surface and satisfying basic conditions for display substrates. However, as glass substrates are heavy and easily broken, researchers studied colorless and transparent plastic polyimide films to replace glass substrates for their excellent thermal and chemical stability.
Nonetheless, colorless and transparent polyimide films do not have sufficient heat resistance and mechanical solidity. To resolve this problem, polyimide films are impregnated with glass-fiber fabrics, but it was far from commercialization as the impregnation exacerbates the roughness of surface and light transmittance. The roughness of the surface increases as the solvent evaporates in the impregnation process, resulting in surface roughness of around 0.4μm. The downturn in light transmittance is due to light scattering effect by the discording refractive index of polyimide film and glass-fiber fabric.
Professor Yoon’s research team resolved these issues by tuning the refractive indices of transparent polyimide film and glass-fiber fabric up to four decimal places, and by developing the technology of flattening the film’s surface roughness to a few nanometers. As a result, the research team achieved heat expansivity of 11ppm/℃, surface roughness of 0.9nm, tensile strength of 250MPa, bending curvature radius of 2mm, and light transmittance at 90% with a 110μm-thick glass-fiber fabric impregnated transparent polyimide film substrate.
“The developed substrate can not only replace the traditional glass substrate but also be applied as flexible display substrate,” said Professor Yoon in prospect, “it will bring about technological innovation in display industry as it can fundamentally resolve the issue of shattering mobile phone displays, reduce the weight and thickness of large-area televisions, and apply Roll to Roll process in display manufacture.”
Supported by the Ministry of Knowledge Economy for five years, the technology has applied for 3 patents and is in discussion for technology transfer with related business.
Figure 1. The according (left) and discording (right) refractive indices of glass-fiber fabric and polyimide film. The characters on the left are sharp and clear, but the characters on the right appear foggy.
Figure 2. Picture of the developed glass-fiber fabric
2013.06.09 View 9259 -
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 13871 -
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 9428 -
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 9459 -
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 19048 -
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 11722