Today I’d like to address three intriguing issues on protein studies that are worth understanding for biological scientists in general: i) how are the proteins endowed with cellular functions of genes; ii) what is the design of conformational changes of the proteins that are crucial to the execution of functions; and iii) what are the current limits in browsing proteome expression as a whole? While the main role of DNA is conveying information coded into genes, the role of the proteins is implementation and coordination of cellular functions, which are manifested as physiology of an organism. Protein functions are determined by their tertiary (3D) structures, more specifically by conformational changes of 3D structures. The amino acid sequence of proteins, which is coded by gene sequence, determines unique 3D structure of the proteins. The process is called ‘protein folding.’ The nature explores structural design of proteins including folding process to endow proteins with biological functions. These two issues, protein folding and design, are addressed by our research on a serine protease inhibitor called antitrypsin. The native functional form of antitrypsin is not a thermodynamically most stable form but a kinetically trapped folding intermediate. We showed that such kinetic block (trap) is a functional design of the nature because strain of the molecule is utilized to facilitate the conformational change needed for the inhibitory function. The last issue, proteomics approach, has been considered a revolutionary technology, especially for discovering phenotype-based biomarker candidates for disease diagnosis and drug responses. While tremendous developments have been achieved recently in proteome separation and mass spectrometry (MS), the current technology of analyzing the whole proteome including PTM (post-transaltional modification) in a quantitative manner is still very challenging. The key criteria here are: how much portion of target proteins the technology can cover and how accurately the analysis quantify the proteome level. To fulfill the above rosy expectations that the proteomic studies aroused, the field needs full conversion from discovering mode into browsing mode, at least for the protein components involved in a specific cellular network under study. The MRM (multiple reaction monitoring)-MS technology, which was adapted to peptides (proteotypic peptides: protein surrogates), has been developed for this purpose. I’ll briefly introduce recent efforts of an international collaboration launched with the goal of developing 1000 MRM assays.
Awards and Honors
- CRS Jorge Heller JCR Award (2012) from the Controlled Release Society for pioneering research on remote controllable drug delivery and BBB crossing demonstration.
- The 1st UNESCO-L’OREAL Award 1998, UNESCO, Paris
- The 50th Seoul City Cultural Award 2001, Seoul City
- Member of The National Academy of Science and Technology(2002 ~ present)
- The Role Models in Science 2003, Korea Science Foundation & DongaScience
- The Order of Science and Technology Merit, Ungbi Medal 2004, Republic of Korea
- 60 Women in 60 Years History of UNESCO 2006, UNESCO, Paris
- Member of The National Academy of Engineering of Korea 2014-2016, The National Academy of Engineering of Korea