051. 629. 5587
- PERSONAL & CONTACT INFORMATION
부경대학교 화학과 해양분자구조생화학 연구실
부산광역시 남구 용소로 45 (608-737)
Rm 5407, Natural Sciences Bldg. I
Department of Chemistry, Pukyong National University
45, Yonso-ro, Nam-Gu, Busan 608-737, Republic of Korea
e-mail : email@example.com
phone : 051-629-5587
Mobile : 101-7178-9024
Ph.D. Washington State University, Department of Biochemistry and Biophysics (2003)
M.S. Pukyong National University, Department of Microbiology (1996)
B.S. Pukyong National University, Department of Microbiology (1994), Graduation with Honors (Summa Cum Laude)
- PROFESSIONAL EXPERIENCE
Assistant Professor, Department of Chemistry, Pukyong National University (2013 ~ 현재)
Principal Research Scientist, Korea Polar Research Institute (2006 ~ 2013)
Adjunct Associate Professor, Department of Polar Science, University of Science and Technology (과학기술연합대학원대학교) (2009.09 ~2013.08)
Lecturer, Department of Chemistry, Hankuk University of Foreign Studies (2008.09 ~ 2009.02)
Postdoctoral Fellow, Vanderbilt University (2003.10 ~ 2006.09)
Teaching and research assistant, Washington State University (1999 ~2003)
Researcher, Bioneer Ltd. (1997 ~ 1998)
Researcher, Vilac Ltd. (1995 ~ 1996)
- Awards and Grants
Davinci Young Scientist Award Grand Prize, Korea Research Council of Fundamental Science & Tecnology (2010)
PKNU alumni association award in Graduation Ceremony (1992)
I. Antifreeze Proteins (Ice-Binding Proteins*): Structure, Function, and Applications
Antifreeze proteins (AFPs) are proteins that depress the freezing point but not the melting point of aqueous solutions by inhibiting the growth of ice crystals. The difference between the freezing and melting points is called thermal hysteresis (TH). The intriguing activity of AFPs has drawn interest from academia and industries because these proteins have broad potential applications, including cryopreservation, food preservation, transgenic technology, and cryosurgery (Davies, P.L. et al. 1989; Hew, C.L. et al. 1992; Wohrmann, A. 1996; Barrett, J. 2001; Ben, R.N. 2001; Bouvet, V. & Ben, R.N. 2003; Harding, M.M. et al. 2003; Fuller, B.J. 2004).
* Ice-binding protein (IBP) is a broad term describing any protein that binds to ice. IBPs include antifreeze proteins (AFPs), proteins that inhibit ice recrystallisation (IRIPs), proteins that anchor something to ice, and possibly even ice nucleation proteins (INPs). However, AFP is somewhat of a misnomer because this type of protein does not prevent freezing. Hence, in some of the literature, AFPs have been termed TH proteins (THPs), according to their activity, or ice structuring proteins (ISPs), since they control the shape and size of ice crystals. However, in much of the literature, IBP and AFP are interchangeable terms because further investigation of IBPs has revealed that, in most cases, they possess TH activity.
1. EPSP synthase and Shikimate Kinase
5-enolpyruvylshikimate-3-phosphate (EPSP) synthase is located in the shikimate pathway (Figure 1), which occupies a key position in providing the biosynthetic route to phenylalanine, tyrosine and tryptophan in bacteria, fungi, algae and higher plants but not in mammals. In addition, a number of other benzenoid primary and secondary metabolites, such as the isoprenoid quinines, and ρ-aminobenzoic acids (PABA), are provided by branch metabolism from this pathway.
EPSP synthase (E. C. 2. 5. 1. 19) catalyzes the unusual reversible transfer of the enolpyruvyl moiety of PEP to 5-OH of S3P to form EPSP and inorganic phosphate via a tetrahedral intermediate (Scheme 1 A). For more than two decades, EPSP synthase has attracted the attention of researchers from agricultural industries and academia for the following reasons. Firstly, EPSP synthase is the target of glyphosate, the active ingredient of the broad spectrum post-emergence herbicide Roundup™ that is used worldwide to control weeds. Secondly, since the shikimate pathway is absent in mammals, EPSP synthase is an intriguing target for the development of new antibiotics and antiparasitics in the advent of antibiotic resistant pathogens such as Staphylococcus aureus and Streptococcus pnuemoniae.
2. Cold-active Proteins
1. Purification, characterization and preliminary X-ray diffraction analysis of a cold-active lipase (CpsLip) from the psychrophilic bacterium Colwellia psychrerythraea 34H. Do HW, Lee JH, Kwon MH, Song HE, An JY, Eom SH, Lee SG, and Kim HJ. (2013) Acta Crystal. F69, 920-924. (I.F: 0.551)
2. Antifreeze Peptides and Glycopeptides, and Their Derivatives: Potential Uses in Biotechnology. Bang JK, Lee JH, Murugan RN, Lee SG, Do HW, Koh HY, Shim HE, Kim HC, and Kim HJ. (2013) Marine Drugs 11(6), 2013-2041.
3. Optimization of the pilot-scale production of an ice-binding protein by fed-batch culture of Pichia pastoris. Lee JH, Lee SG, Do H, Park JC, Kim E, Choe YH, and Kim HJ. (2013) Appl. Microbiol. Biotechnol. 97, 3383-3393.
4. Frozen assembly of gold nanoparticles for rapid analysis of antifreeze protein activity. Park JI, Lee JH, Gwak Y, Kim HJ, Jin ES, and Kim Y.P (2013) Biosens. Bioelectron. 41, 752-757.
5. Peptoid-based positional scanning derivatives: revealing the optimum residue required for ice recrystallization inhibition activity for every position in the AFGPs. Ahn M, Murugan RN, Shin SY, Kim HJ*, and Bang JK*. (2012) Bull. Kor. Chem. Soc. 33(12), 3931-3932. (I.F: 0.936) (Co-corresponding authors)
6. Synthesis of cyclic antifreeze glycopeptide and glycopeptoids and their ice recrystallization inhibition activity. Ahn M, Murugan RN, Shin SY, Kim E, Kim HJ*, and Bang JK*. (2012) Bull. Kor. Chem. Soc. 33(11), 3565-3570. (I.F: 0.936) (Co-corresponding authors)
7. Draft Genome Sequence of Paenisporosarcina sp. Strain TG-20, a Psychrophilic Bacterium Isolated from the Basal Ice of Taylor Glacier, McMurdo Dry Valleys, Antarctica. Lee JH, Koh, HY, Lee SG, Doyle S, Christner BC, and Kim HJ. (2012) J. Bacteriol. 194(23), 6636. (I.F: 3.924)
8. Draft Genome Sequence of Paenisporosarcina sp. Strain TG-14, a Psychrophilic Bacterium Isolated from Sediment-Laden Stratified Basal Ice from Taylor Glacier, McMurdo Dry Valleys, Antarctica. Koh, HY, Lee SG, Lee JH, Doyle S, Christner BC, and Kim HJ. (2012) J. Bacteriol. 194(23), 6656-6657. (I.F: 3.924)
9. Draft genome sequence of Moritella dasanensis strain ArB 0140, a psychrophilic bacterium isolated from the Arctic ocean. Lee SG, Koh HY, Lee JH, Kang S-H and Kim HJ. (2012) J. Bacteriol. 194(19), 5452-5453. (I.F: 3.924)
10. Studies on the effect of number of sugar moiety in the antifreeze activity of homodimeric AFGPs. Ahn M, Murugan RN, Kim E, Lee HJ, Cheong C, Kang SW, Park HJ, Shin SY, Kim HJ*, and Bang JK*. (2012) Bull. Kor. Chem. Soc. 33(7), 2411-2414. (I.F: 0.936) (Co-corresponding authors)
11. Crystallization and preliminary X-ray crystallographic studies of the ice-binding protein (FfIBP) from Flavobacterium frigoris PS1. Do HW, Lee JH, Lee SG, and Kim HJ. (2012) Acta Crystal. F68(7), 806-809. (I.F: 0.551)
12. Two type I crustacean hyperglycemic hormone (CHH) genes in Morotoge shrimp (Pandalopsis japonica): Cloning and expression of eyestalk and pericardial organ isoforms produced by alternative splicing and a novel type I CHH with predicted structure shared with type II CHH peptides. Jeon JM, Kim BK, Lee JH, Kim HJ, Kang CK, Mykles DL, and Kim HW. (2012) Comp. Biochem. Physiol. 162(4), 88-99. (I.F: 2.196)
13. Analysis of expressed sequence tags from the Antarctic psychrophilic green algae, Pyramimonas gelidicola. Jung W, Lee SG, Kang SW, Lee YS, Kang S-H, Jin ES* and Kim HJ*. (2012) J. Microbiol. Biotechnol. 22(7), 902-906. (I.F: 1.463) (Co-corresponding authors)
14. Cryopreservative effects of the recombinant ice-bining protein from the Arctic yeast Leucosporidium sp. on red blood cells. Lee SG, Koh HY, Yoon SR, Lee JH, Kang S-H and Kim HJ. (2012) Appl. Biochem. Biotechnol. 167(1) 824-834.
15. Structural basis of antifreeze activity of ice-binding protein from Arctic yeast Leucosporidium sp. Lee JH, Park AK, Do HW, Park KS, Ji YM and Kim HJ. (2012) J. Biol. Chem. 287(14), 11460-11468. (I.F: 5.328)
16. Characterization of ice-binding protein from Arctic yeast Leucosporidium sp. Park KS, Do HW, Lee JH, Park SI, Kim E, Kang S-H and Kim HJ. (2012) Cryobiology 64(3) 286-296. (I.F: 1.718)
17. Possible role of horizontal gene transfer in the colonization of sea ice by algae. Raymond JA and Kim HJ. (2012) Plos One 7(5), e35968. (I.F: 4.351)
18. Full genome analysis of a novel adenovirus from the South Polar skua (Catharacta maccormicki) in Antarctica. Park YM, Kim J-H, Gu SH, Lee SY, Lee M-G, Kang YK, Kang S-H, Kim HJ and Song J-W. (2012) Virology 422, 144-150. (I.F: 3.042)
19. A modified cryopreservation method of psychrophilic chlorophyta Pyramimonas sp. From Antarctica. Hong SS, Lee SY, Kim YN, Kang S-H and Kim HJ. (2011) Ocean Polar Res. 33(3), 303-308.
20. 구조생물학을 이용한 Antifreeze protein의 최근 연구동향. Lee JH, Lee SG, and Kim HJ. (2011) Ocean Polar Res. 33(2), 159-169.
21. Crystallization and preliminary X-ray crystallographic studies of the ice-binding protein from the Arctic yeast Leucosporidium sp. AY30. Park AK, Park KS, Kim HJ, Park H, Ahn IY, Chi YM and Moon JH. (2011) Acta Crystal. F67, 800-802. (I.F: 0.551)
22. Crystallization and preliminary X-ray crystallographic analysis of the human kindlin-2 PH domain. Lee JH, An JY, Park HJ, Kim HJ, and Eom SH. (2011) Acta Crystal. Section F. 67, 696-699. (I.F: 0.551)
23. Molecular and comparative analyses of type IV antifreeze proteins (AFPIVs) from two Antarctic fishes, Pleuragramma antarcticum and Notothenia coriiceps. Lee JK, Kim, YJ, Park KS, Sin SC, Kim HJ, Song YH, and Park H. (2011) Comp. Biochem. Physiol. 60(20), 222-228. (I.F: 2.196)
24. The structural flexibility of the shank1 PDZ domain is important for its binding to different ligands. Lee JH, Park HJ, Park SJ, Kim HJ, and Eom SH. (2011) Biochem. Biophys. Res. Comm. 407, 207-212. (I.F: 2.548)