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< Si-hyun Ham, a world-class protein specialist and professor in chemistry >

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​Si-hyun Ham, a professor in chemistry at our university is recognized as a world-class protein specialist. Her specialty is focused on obstinate diseases such as dementia, diabetes, cancer and Parkinson disease, and nowadays she strives to reveal the causes of protein aggregation that brings about obstinate diseases. In 2012 she revealed the mechanism of protein aggregation relating to the occurrence of dementia for the first time in the world, and in recent times she has revealed a new cause of protein aggregation. Since then, the world have been taking note, and in 2014 she has brought off something again.

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Her new treatise was carried in the on-line edition of a chemical journal of world authority ‘Angewandte Chemie International Edition’ on February 24th, and its importance was highly evaluated and has been on the cover. The treatise has been ranked in the top 10% of ones carried in the journal and thus selected as a highly important paper(HIP). Additionally, this spring, SAMSUNG put her name to the top of the list of ‘notable Korean scientists’ as part of its Future Technology Development Project. Her work is sufficient to be chosen as the cover model of ‘SOOKMYUNG’ university newsletter.​

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The​ science of convergence let the world know computational chemistry

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Computational chemistry is the key to the understanding of her study. Literally, it means that chemical experiments are conducted in the supercomputer, not in the laboratory. For that reason, it’s another name is ‘theoretical chemistry.’ Chemistry met the computer and created a new field, which was met with the buzzword ‘convergence.’ Modern sciences have difficulty staying on as independent fields anymore, and accordingly they need to interlock with each other and be complementary to each other; in other words, we are living in an age of convergence. The 2013 Nobel prize in chemistry well shows such a trend, because it fell to scientists who developed a simulation program to computethe chemical reactions of complicated and large biomolecules. In brief, Prof. Ham’s computational chemistry is one of the hottest issues of the 21st century.

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​Creative thinking has revealed the mechanism of protein aggregation

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"I study protein at my desk or on my bed, not in the laboratory, using my notebook connected to a supercomputer. Our contemporaries’ obstinate diseases are typified by dementia and cancer, most of which are related to protein aggregation. When protein accumulates abnormally, it forms agglomerates, which is called ‘protein aggregation.’Many studies are underway to control what protein agglomerates, but most of them are focused on the properties of protein and thus have not produced significant results. This is why I had to find a new way to comprehend and predict the mechanism at the molecular level, and finally our team made it.”

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A key to her success is thinking outside of the box. All centered around protein itself, but she focused on the interaction between protein and water, having views upon whatwater accounts for the highest percentage of body composition.Her method makes it possible to calculate the structure and distribution of water around protein and to predict why and how much protein agglomerates. It has about 90% accuracy. As protein aggregation that leads to the occurrence of a disease can be controlled at the molecular level, her study offered some approach to the development of medicines in addition to the comprehension of related diseases. “In developing a new medicine against a disease caused by protein aggregation, the first consideration is to design the medicine, and it involves a computer simulation to know which type is more efficacious. Also, the computer simulation saves time and costs. It suggests the first possible approach to design non-aggregated protein at the molecular level. It’s possible to apply this technology right away.”

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Prof. Ham paraphrases that process into ‘design.’The medicine should be convex-shaped in order that it can be engaged with the active site of protein, a concave shape, and vice versa. It is hard and boring to calculate the structure of the medicine to be engaged with protein having the uneven and complicated shape, but nevertheless, she calls that work ‘design’. It witnesses to her getting enjoyment from her work. All she does can be expressed as ‘fever’ and it is similar to an impression given by a person who is crazy about something.

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Remember the sweat and tears in the title ‘a world-class scientist’

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The relationship between Prof. Ham and our university reaches back very far. In 1991 she graduated at the top of the chemistry department at our university, and in 1993 left for Texas Tech University. Then, she came back to our university, holding a chair. At that time she was at the age of 33. She had a bright future but sped homeward as her father fell sick. She came back to our university dramatically, and 10 years have passed since then. In those days our university was unfamiliar with computational chemistry, but she opened the class of computational chemistry (chemoinformatics) in 2004 and has been giving lectures to students passionately ever since.

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Computational chemistry is tricky for undergraduate studies, and it is rarelyoffered locally and abroad. No doubt, however, she believed that her juniors would do it better than anyone. Now, 10 years later, her disciples are receiving attention from companies developing bio medicines and government-affiliated research institutes. Nowadays, computational chemistry is applied not only to bioscience and medicines but to nano-engineering, material engineering, cosmetics, clothing, environment and otherwise.

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Though she has been a world-class scientist, she is still keen on doing his work. Even now she is throwing herself into treatment for obstinate diseases, giving up her daily life. She said to her juniors that they cannot make it without courage. We are rooting for her.

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