Tel: (office) +82-42-350-2844, (lab) +82-42-350-2884
Location: (office) Room 505 (Bldg. E6-6), (lab) Room 513, 514 (Bldg. E6-6)
Fax: +82-42-350-2810

Ph. D. Chemistry, California Institute of Technology June, 2001(Graduate Advisor: Prof. Ahmed H. Zewail)
B. S. Chemistry, KAIST(Korea Advanced Institute of Science and Technology) February, 1994
Graduated with highest honor (2nd out of 550 graduates)

· Professor, Department of Chemistry, KAIST 2009 - present
· Associate Professor, Department of Chemistry, KAIST 2006 - 2009
· Assistant Professor, Department of Chemistry, KAIST 2003 - 2006
· Group Leader, Center for Nano-materials & Chemical Reactions 2012 - present
(Institute for Basic Science)
· Director, Center for Time-Resolved Diffraction 2007 - 2012
(National Creative Research Initiatives by MOST/KOSEF)
· Postdoctoral Scholar (Prof. K. Moffat) 2001 - 2003
Department of Biochemistry &Molecular Biology, University of Chicago
· Postdoctoral Scholar (Prof. A. H. Zewail) 2001
Department of Chemistry, California Institute of Technology
· Graduate Research Assistant (Prof. A. H. Zewail) 1994 - 2001
Department of Chemistry, California Institute of Technology
Research Advisor: Prof. A. H. Zewail
Research Collaborator: Prof. W. A. Goddard, III

· American Crystallographic Association 2008 - present
· American Association for the Advancement of Science 1998 - present
· American Physical Society 1996 - present
· American Chemical Society 1994 - present

· Morino Lectureship Award (MEST) 2011
· Best Lecturer Award (KAIST Chemistry Department) 2010
· Lectureship Award from Chemical Society of Japan 2009
· KAIST Teaching Excellence Award 2009
· KAIST Teaching Excellence Award 2008
· Best Oral Paper at 10th Eurasia Conference on Chemical Sciences 2008
· Best Lecturer Award (KAIST Chemistry Department) 2006
· 10th Young Scientist Award (MOST/KIAS) 2006
· 16th KOFST Best Paper Award 2006
· KAIST Academic Excellence Award 2006
· Damon Runyon Cancer Research Fellow 2002 - 2003
· Graduated with highest honors from KAIST 1994

One of the most fundamental questions in biology, chemistry, and physics is how the molecules interact, so called, reaction mechanisms. Our laboratory strives to understand the reaction mechanisms in molecular detail in gas phase, solution phase, and solid phase spanning amorphous phase, polycrystalline and single crystals. Traditionally, femtosecond spectroscopy has been used to achieve this goal, however, spectroscopic data, in most cases, fail to provide direct information on the structural changes such as bond lengths and bond angles. To remedy this, we combine the traditional femtoscience with direct structural tools such as diffraction, EXAFS, and NMR. These techniques can be applied to a wide range of systems, encompassing small molecules, nano-scale complexes, and macromolecules such as polymers, proteins and DNA. A typical experiment is conducted in a pump-probe manner; an optical pulse such as femtosecond laser pulse is directed to the sample of interest to initiate a desired reaction, and after a well-defined time delay, a probing pulse such as an ultrashort x-ray pulse is sent to the sample undergoing a reaction. Then, the signal resulted from the interaction of the reacting system and the probing pulse captures the molecular actions in real time. Since the measured signal (in this case, diffraction signal) is a function of molecular structures, the time-dependant data at various time delays contains a clue to the molecular reaction mechanisms and a novel data analysis of the time-resolved signal finally reveals the mechanism.

· Molecular structural Dynamics
· Chemical Reaction Dynamics
· Protein structural Dynamics
· Ultrafast X-ray Diffraction
· Ultrafast Electron Diffraction
· Ultrafast spectroscopy

"Volume-conserving trans-cis isomerization pathways in photoactive yellow protein visualized by picosecond X-ray crystallography", Y. O. Jung, J. H. Lee, J. Kim, M. Schmidt, K. Moffat, V. Srajer, H. Ihee*, Nature Chemistry, in press (2013)
"Direct observation of cooperative protein structural dynamics of homodimeric hemoglobin from 100 picoseconds to 10 milliseconds with pump-probe X-ray solution scattering", K. H. Kim, S. Muniyappan, K. Y. Oang, J. G. Kim, S. Nozawa, T. Sato, S. Koshihara, R. Henning, I. Kosheleva, H. Ki, Y. Kim, T. W. Kim, J. Kim, S. Adachi, H. Ihee*, J. Am. Chem. Soc., 134, 7001-7008 (2012).
"Protein structural dynamics of photoactive yellow protein in solution revealed by pump-probe X-ray solution scattering", T. W. Kim, J. H. Lee, J. Choi, K. H. Kim, L. van Wilderen; L. Guerin, Y. Kim, Y. O. Jung, C. Yang, J. Kim, M. Wulff, J. van Thor*, H. Ihee*, J. Am. Chem. Soc., 134, 3145-3153 (2012)
"Visualizing Solution-Phase Reaction Dynamics with Time-Resolved X-ray Liquidography", H. Ihee*, Acc. Chem. Res., 42, 356-366 (2009)
"Tracking the structural dynamics of proteins in solution using time-resolved wide-angle X-ray scattering.", M. Cammarata*, M. Levantino , F. Schotte, P. A. Anfinrud, F. Ewald, J. Choi, A. Cupane, M. Wulff, H. Ihee*, Nature Methods, 5, 881-887 (2008)
“Initial Catalyst-Substrate Association Step in Enyne Metathesis Catalyzed by Grubbs Ruthenium Complex Probed by Time-Dependent Fluorescence Quenching", J.-H. Sohn*, K. H. Kim, H. Y. Lee, Z. S. No, H. Ihee*, J. Am. Chem. Soc., 130, 16506-16507 (2008)
"Ultrafast X-ray diffraction of transient molecular structures in solution", H. Ihee*, M. Lorenc, T. K. Kim, Q. Y. Kong, M. Cammarata, J. H. Lee, S. Bratos, M. Wulff, Science, 309, 1223-1227 (2005)