Science
-
Complex responsible for protein breakdown in cells identified using Bio TEM
Professor Ho-Min Kim
- High resolution 3D structure analysis success using Bio Transmission Electron Microscopy (TEM), a giant step towards new anticancer treatment development
- Published in Nature on May 5th
Using TEM to observe protein molecules and analysing its high resolution 3D structure is now possible. KAIST Biomedical Science and Engineering Department’s Professor Ho-Min Kim has identified the high resolution structure of proteasome complexes, which is responsible for protein breakdown in cells, using Bio TEM.
This research has been published on the world"s most prestigious journal, Nature, online on May 5th. Our body controls many cellular processes through production and degradation of proteins to maintain homeostasis. A proteasome complex acts as a garbage disposal system and degrades cellular proteins when needed for regulation, which is one of the central roles of the body.
However, a mutation in proteasome complex leads to diseases such as cancer, degenerative brain diseases, and autoimmune diseases.
Currently, the anticancer drug Velcade is used to decrease proteasome function to treat Multiple Myeloma, a form of blood cancer. Research concerning proteasome complexes for more effective anticancer drugs and treatments with fewer side effects has been taking place for more than 20 years. There have been many difficulties in understanding proteasome function through 3D structure analysis since a proteasome complex, consisting of around 30 different proteins, has a great size and complexity.
The research team used Bio TEM instead of conventionally used protein crystallography technique. The protein sample was inserted into Bio TEM, hundreds of photographs were taken from various angles, and then a high–performance computer was used to analyse its structure. Bio TEM requires a smaller sample and can analyse the complexes of great size of proteins.
Professor Ho-Min Kim said, “Identifying proteasome complex assembly process and 3D structure will increase our understanding of cellular protein degradation process and hence assist in new drug development using this knowledge.” He added, “High resolution protein structure analysis using Bio TEM, used for the first time in Korea, will enable us to observe structure analysis of large protein complexes that were difficult to approach using protein crystallography.” Professor Kim continued, “If protein crystallography technology and Bio TEM could be used together to complement one another, it would bring a great synergetic effect to protein complex 3D structure analysis research in the future.”
Professor Ho-Min Kim has conducted this research since his post-doctorate at the University of California, San Francisco, under the advice of Professor Yifan Cheng; in co-operation with Harvard University and Colorado University.
Figure 1: A picture taken by Bio TEM of open state protein sample (proteasome complex)
Figure 2: Bio TEM image analysis showing protein 3D structure
2013.05.25 View 10233 -
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 8557 -
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 10386 -
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 9413 -
Op-Ed by Prof. David Helfman: Global Science and Education in the 21st Century
Professor David Helfman from the Department of Biological Sciences and Graduate School of Nanoscience and Technology(https://sites.google.com/site/cellsignalinglaboratory/home) recently wrote an Op-Ed in the January 2013 issue of Journal of Happy Scientists and Engineers that ispublished by the Ministry of Science, Education and Technology, the Republic of Korea. In the article entitled “Global Science and Education in the 21st Century,” Professor Helfman addressed three important issues in science and education, which will have a great impact for the development of world-leading universities in Korea. For the article, please see the attachment.
2013.01.22 View 10913
-
Ph.D. students Hyowon Park and Won Ma receive Grand Prizes in Mathematics and Biology respectively.
Researchers in KAIST received best paper awards in two out of three fields at this year’s award ceremony for the “Second Annual Best Thesis Paper Award” held collectively by the Korea University Presidents’ Federation (with Chairman DaeSoon Lee) and the Korean Academy of Science and Technology (with Director GilSang Jung).
Two researchers from KAIST, Hyowon Park (Department of Mathematics) and Won Ma (Department of Biology) received best paper awards.
This prize, given by the both the Korea University Presidents’ Federation and the Korean Academy of Science and Technology since last year, is awarded to researchers and assistant professors who write the most outstanding thesis papers in the field of basic sciences.
Park, who received the best paper award this year, did research on graph braid groups. He was supervised by Professor Kihyung Ko, who received the best supervisor reward.
Ma, who received the best paper award in the field of biological science, researched about the Attention Deficit/Hyperactivity Disorder due to deficiency of the GIT1 synapse protein. His supervising professor also received the supervisor award.
The award ceremony was held in the auditorium of the S-OIL headquarters in Seoul on November 30.
Meanwhile, NASA researcher Jaehwa Lee received the best paper award in the field of earth science, and his supervising professor, Professor Jun Kim from Yonsei University who studies atmospheric science, received the best supervisor award.
2012.12.21 View 9565
-
Novel material that prevents health decline with age found
Professor Kim Dae Soo (Department of Biological Science), his research team, the Choong Nam University Medicine School, and various companies conducted collaborative research succeeded in developing a novel material that prevents health decline with age. The result was published in PLoS One Journal with the title “Beta-lapachone, a modulator of NAD metabolism, prevents health declines in aged mice”.
Longevity and health can be obtained with reducing consumption of food and aerobic exercise.
Professor Kim’s team focused on the fact that reduced consumption of food and aerobic exercise increase the coenzyme (NAD+) which suppresses the aging of cells. The research team discovered that by activating NQO1 enzyme with Beta-lapachone, the amount of NAD+ in the body increases even without reduction of food consumption or aerobic exercise.
Even consumption of Beta-lapachone by aging mice caused an improved on the brain and exercise ability of the mice. It is expected that commercialization of Beta-lapachone will be possible as it is a chemical that is commonly found in herbs used in both the orient and the oxidant.
2012.12.21 View 6987
-
The 2nd 'Humanities Lecture for Citizens" to be held
The Department of Humanities and Social Sciences (HSS) at KAIST will hold its 2nd ‘Humanities Lecture for Citizens’, making high level humanities and social science programs available to ordinary citizens.
The program will start on October 16th and will provide one lecture a week for 8 weeks. The lectures will start every Tuesday from 3pm to 5pm at the KAIST international conference room in the N4 building.
The lecture topics include love, psychology, food culture, public opinion, gender and technology- issues that are widely cited throughout society, but are hard to define. The program will end with field trips to the Daejeon Museum of Art and the Ungno Lee Museum of Art.
Professor Shin Dong Won, who managed the program said that ‘this will be a great opportunity for citizens to participate in HSS lectures and to self reflect on social matters.
Lecture Topics (in Korean)
이원재 KAIST 문화기술대학원 교수 <사랑의 역설과 소셜 네트워크>
김정훈 KAIST 인문사회과학과 교수 <심리학적 지식의 불편한 진실>
이석봉 대덕넷 대표 <디지털 시대의 아날로그 해법 ‘종이 신문’>
김동주 KAIST 인문사회과학과 교수 <우리 시대의 먹거리 문화에 대한 성찰 : 고대 인류는 무엇을 먹고 살았을까?>
신피터경섭 KAIST 인문사회과학과 교수<삼성 대 애플, 최후의 승자는?>
박현석 KAIST 인문사회과학과 교수 <여론 조사와 대통령 선거: 과연 국민의 뜻은 무엇인가?>
윤정로 KAIST 인문사회과학과 교수 <여성의 눈으로 본 과학 기술>
김원준 KAIST 경영과학과 교수가 <요즘 왜 자꾸 통섭, 융합이 화두인가?>
2012.10.20 View 6527
-
Professor Yoon Dong Ki becomes first Korean to Receive the Michi Nakata Prize
Professor Yoon Dong Ki (Graduate School of Nano Science and Technology) became the first Korean to receive the Michi Nakata Prize from the International Liquid Crystal Society.
The Awards Ceremony was held on the 23rd of August in Mainz, Germany in the 24th Annual International Liquid Crystal Conference.
The Michi Nakata Prize was initiated in 2008 and is rewarded every two years to a young scientist that made a ground breaking discovery or experimental result in the field of liquid crystal. Professor Yoon is the first Korean recipient of the Michi Nakata Prize.
Professor Yoon is the founder of the patterning field that utilizes the defect structure formed by smectic displays. He succeeded in large scale patterning complex chiral nano structures that make up bent-core molecules.
Professor Yoon’s experimental accomplishment was published in the Advanced Materials magazine and the Proc. Natl. Acad. Sci. U.S.A. and also as the cover dissertation of Liquid Crystals magazine.
Professor Yoon is currently working on Three Dimensional Nano Patterning of Supermolecular Liquid Crystal and is part of the World Class University organization.
2012.09.11 View 11282
-
Professor Kim Eun Joon receives In Chon Award
Professor Kim Eun Joon (Department of Biological Sciences) received the In Chon Awarded hosted by In Chon Memorial and Dong Ah Newspaper.
The Award Ceremony will be held on the 8th of October in Seoul Lotte Hotel and Professor Kim will be given a medal and prize money amounting 100million Korean Won.
Professor Kim is a world renowned research in the field of Synapses. Professor Kim graduated from the Department of Pharmacy in Pusan University, B.A. at KAIST, and Ph.D at Michigan University. He has been a Professor at KAIST since 2000.
2012.09.11 View 7820
-
Hosting of Third Annual 2012 Social Web International Workshop
KAIST Department of WebScience Engineering hosted the 2012 Social Web International Workshop in JaeJu Ramada Hotel.
The 3rd Annual International Workshop involves the coming together of domestic and international experts on various fields like sociology, journalism, electronics, economics, and etc. to introduce and discuss the direction of social web’s numerous factions.
Dr. Krishna Gummadi (Max Plank Research Institute), Professor Irwin King (Chinese University of Hong Kong), Dr. Winter Mason (Stevens Technology Research Institute), and Professor Daniele Quercia (Cambridge University) made up the international participants of the workshop.
Professor Kim Yong Chan (Yonsei University), Professor Kim Ye Ran (KwangWoon University), Professor Park Ju Yong (Kyung Hee University), Professor Oh Hae Yeon and Professor Lee Won Jae (KAIST) made up the domestic participants to the workshop.
The workshop was a place for free discussion of social networks and apps and the research direction of social sciences.
2012.08.21 View 7242
-
Ultra Elastic Electrode Material Developed
KAIST research team succeeded in developing the next generation flexible and elastic electrode material crucial in the development of flexible displays, wearable computers, and etc.
Professor Jeon Seok Woo’s team of the department of Materials Science and Engineering succeeded in the development of a super elastic material.
The result of the experiment was introduced as the research highlight in Nature Communications and is especially significant as the main driving force behind the achievement were domestic researchers.
Professor Jeons team developed a structured three dimensional nano-porous structure over a 1inch by 1inch area that is 10micrometers in thickness. The structure is fabricated using world’s largest area three dimensional nano patterning technique.
The nano-porous structure was injected with elastomeric material and was subsequently removed to yield an inverse three dimensional elastic nano material. The pores were infiltrated with liquid conductive material which yielded a super elastic flexible electrode.
The fabricated electrode showed amazing elasticity levels and was able to light LED lamps in a 200% stretched state without decrease in electrical conductivity.
Conventional methods included folding and expanding a material like an accordion or creating a mesh-like structure by making holes in the material. However these methods yielded materials with limited elasticity and even 100% stretching resulted in the drastic decrease in electrical conductivity.
Professor Jeon expects the domestically developed technology to obtain the upper hand in the market and make great contributions in both science and society.
2012.07.26 View 8962