For the fifth year in a row, Mei Hong, assistant professor of chemistry,
has won a major award.
This time it’s the Alfred P. Sloan Research Fellow, 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.
"This is an extraordinarily competitive award, involving nominations
for most of the very best scientists from this generation from around
the world," writes Ralph Gomory of the Sloan Foundation. "Your
(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."
Funds may be used for support of pre or postdoctoral research assistants,
supplies, equipment, professional travel, and other expenditures directly
related to Hong’s research.
Awards every year have become a habit of Hong’s. Her string of honors
began while she was on the faculty at the University of Massachusetts
at Amherst when in 1998 the National Science Foundation (NSF) granted
her a POWRE Award.
A year later, Hong, by then an assistant professor of chemistry at Iowa
State, received the Beckman Young Investigator Award for innovation. The
award is given annually for research within the chemical and biological
sciences.
In 2000, Hong was honored by the Research Corporation with a Research
Innovation Award.
Then last year, she received a NSF CAREER Award, granted to beginning
principle investigators for both research and educational activities.
"They (CAREER Awards) are known to be extremely competitive, more
than normal NSF grants, so I am very pleased and honored that my proposal
was selected in the first round," Hong said. "This is very encouraging
to our research program."
Hong was awarded a five-year, $500,000 CAREER Award on "Elucidation
of the Conformation and Dynamics of Membrance 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.
"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 will investigate the structure and dynamics
of a 22 kDa antibiotic protein, colicin la channel domain.
"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."
CAREER Awards however aren’t solely about research – they must
have an educational component to them as well. Hong plans to design a
protein structure module for general chemistry to integrate research with
teaching and create web pages for undergraduate physical chemistry courses.
"I hope these educational initiatives will make the undergraduate
chemistry curriculum more fun, more accessible, and more in tune with
the latest developments at the chemistry-biology interface," she
said.
