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UCSB Professor Receives $750,000
updated: Mar 08, 2012, 9:38 AM
Songi Han, associate professor in the Department of Chemistry & Biochemistry at
UC Santa Barbara, has received a $750,000 award from the National Science
Foundation for her research, "IDBR: Novel Electron-Nuclear Dual Resonance
Instrument with Arbitrary Microwave Pulse Shaping to Advance the Structure and
Dynamics Study of Biological Systems."
The project aims to enhance the sensitivity of pulsed electron paramagnetic
resonance (EPR) instruments, spectroscopic tools that offer important analysis
and diagnostic information in the chemical and biomedical fields. While
currently not as highly developed and widely disseminated as sister
technologies, such as Nuclear Magnetic Resonance (NMR) and Magnetic Resonance
Imaging (MRI), EPR technology offers the opportunity to dissect the structures
and functions of large and complex biological systems that often escape the
limits of NMR and MRI diagnosis.
NMR gives the most detailed information of a biomolecule at the atomic level.
But, the level of detail is both its strength and its detriment. Objects under
scrutiny - proteins, for instance - have to be well-defined, not too large, and
"well-behaved," according to Han.
"More often than not, in biology, proteins are part of a messy system," said
Han, adding that they often interact with one another and with other structures.
The real strength of EPR, she said, is its ability to give an overview of large
and complex biological systems, where the tight, close-up focus of NMR and MRI
can't provide useful information on structure and dynamics.
Take, for example, the early and soluble protein aggregates that are thought to
be toxic species, which eventually form amyloid fibrils found in the brain of
Alzheimer's sufferers. These soluble protein oligomers and aggregates are
already too big to be viewed easily by NMR spectroscopy, too ill-defined to be
viewed by X-ray crystallography and too small to be seen by transmission
electron microscopy, said Han. With the degree of control being developed by Han
and her colleagues to refine EPR spectroscopy, these hard-to-see proteins can be
analyzed not just for structure, but also for their interactions in the larger
system, in water, and as a function of environmental factors and time.
The key to accuracy is to control the shapes of the EPR spectroscope's pulses,
which are used to excite the electron spin probes that report on the host
molecule's local structure and their environment. Current technology provides
little control over these pulses, which often result in less-than-accurate
control over the readings. By manipulating the input, said Han, it's possible
to overcome the shortcomings of conventional pulsed EPR measurements.
"In order for me to account for the imperfection of my hardware, I need to shape
my pulses with arbitrary pulse forms," said Han. It would also be possible to
measure very fast-decaying (short-lived) signals of the electron spins of the
biomolecular samples that currently can't be read due to the much slower
reacting artifact originating from the slow pulse response of the conventional
EPR spectroscope. Han's development will potentially push EPR to be a more
mainstream analytical tool, by offering higher sensitivity, higher time
resolution and the need for smaller sample quantities.
The funding from the NSF instrumentation development grant will go toward the
development and applications of the EPR pulse shaping technology, which will
include building, trials and troubleshooting, said Han. She and her group, which
also includes co-principal investigators Mark Sherwin and John Martinis,
professors of physics, are among the few researchers in the world offering
unique microwave technologies essential for this development.
"We think this technology is so sought after and relevant that it has the
potential to be commercialized within the next three years," said Han.
Han, who joined the UCSB faculty in 2004, received her doctoral degree in the
natural sciences from Aachen University of Technology in Germany. She completed
postdoctoral studies at UC Berkeley with the Feodor Lynen Fellowship of the
She is the recipient of numerous honors and awards, including the 2011 NIH New
Innovator Award, the 2010 Dreyfus Teacher-Scholar Award; the 2008 Packard
Fellowship for Science and Engineering; the 2007 National Science Foundation
Early Career Development Award; and the 2004 Camille and Henry Dreyfus New
Comments in order of when they were received | (reverse order)
2012-03-08 10:18 AM
Wow. Amazing career highlights for the whole team. Exciting stuff. A next big step. Go researchers ... and, thank you.
2012-03-08 03:59 PM
All this money and school fees keep going up. Highway robbery...
2012-03-09 07:34 AM
Goodness, I still don't understand what's she's doing, but congratulations!
2012-03-09 11:27 AM
777 - This could very well be a HUGE breakthrough in ability to interpret and manipulate proteins.
$750k is a very small price to pay for such an important bit of work.
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