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Old hat
Another year, another award for chemistry's Mei Hong.
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This has started to become old hat for Mei Hong, associate professor
of chemistry.
For the sixth year in a row, Hong has been honored for her work.
This time it was by the College of Liberal Arts and Sciences, who awarded
Hong its Award for Early Excellence in Research / Artistic Creativity.
The award recognizes faculty members who have demonstrated outstanding
research activities usually early in their professional careers.
And just last week, Hong received the American Chemical Society's Award
in Pure Chemistry. This award recognizes and encourages fundamental research
in pure chemistry carried out in North America by young men and women.
It's just the latest in a series of awards that Hong has received in recent
years. Other awards include:
*2002 - Alfred P. Sloan Research Fellowship, a two-year, $40,000 grant
to be used in a "flexible and largely unrestricted manner to provide
the most constructive possible support" of Hong's research. According
to the Sloan Foundation, this award is extremely competitive and Hong's
"selection conveys a clear indication of the high esteem in which
your past work and future potential are held by your fellow scientists."
* 2001 – National Science Foundation (NSF) CAREER Award, granted
to beginning principal investigators for both research and educational
activities. Hong was awarded a five-year, $500,000 CAREER Award on “Elucidation
of the Conformation and Dynamics of Membrane Proteins by Solid-State NMR.”
The broad objective of her research is to elucidate membrane protein structure
and dynamics using advanced solid-state NMR spectroscopy. Membrane proteins
are associated with the sticky boundaries that separate the cell interior
from the outside. They have a number of essential functions, such as regulating
cellular transport and cell signaling.
*2000 – Research Corporation's Research Innovation Award
* 1999 – Beckman Young Investigator Award for innovation. The award
is given annually for research within the chemical and biological sciences.
* 1998 – NSF POWRE Award granted while she was on the faculty at
the University of Massachusetts at Amherst.
Gordon Miller, professor and chair of the Department of Chemistry, says
Hong's creative research themes "combine development and applications
of nuclear magnetic resonance (NMR), which will be utilized by chemists
in several disciplines for years to come."
Hong's scholarly activity emphasizes the development of new NMR techniques
and their applications to study structure-function relations in biological
systems.
"Knowledge of the three-dimensional structure is the basis for understanding
function," Hong said. "Solid-state NMR is a unique method for
studying membrane proteins, because it allows you to investigate these
proteins directly in their native environment, the lipid bilayer."
Specifically, Hong's group is investigating the structure and dynamics
of a 22 kDa antibiotic protein, colicin la channel domain with the NSF
CAREER funding.
"Colicin is a very facile molecule," Hong said. "It can
change its shape from a water soluble form to something that adapts to
the sticky lipid membrane. This is the first step towards the destruction
of the bacterial cell. We want to know how this structure change occurs.
It’s a fundamental question of protein folding."
Diseases such as cystic fibrosis and "mad cow" disease are caused
by the misfolding or the formation of incorrect three-dimensional structures
of proteins.
"To find a cure for these diseases, it is paramount to elucidate
the three-dimensional structures of proteins," Hong said.
The proteins and peptides that Hong is investigating are generally very
effective with bacteria, so much so that Hong says some of these proteins
are more potent than most current antibiotics.
"Short peptides can be easily made today by pharmaceutical companies,"
Hong said, "and these antibacterial peptides can kill a wide range
of bacteria in a short time. They often do this by opening up a channel
in the (cell's) membrane, but there are also other mechanisms. The bottom
line is, the bacteria can't handle the protein."
Around LAS
September 22 to October 5, 2003
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