College of Liberal Arts and Sciences at Iowa State University

Once a year

If the calendar has moved to another year, it must mean an award for chemistry's Mei Hong.
It's a red-letter day for most of us when we learn that we have received an award.

Red-letter days seem to come every year for Mei Hong, assistant professor of chemistry.

Hong's string of awards 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.

So what does she do for an encore in 2001?

This year, Hong has 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 is the third faculty member of the College of Liberal Arts and Sciences to receive a NSF CAREER Award in 2001. Wallapak Tavanapong, assistant professor of computer science, and Yuhong Yang, assistant professor of statistics, have also been notified they have been selected for the prestigious grant.

Hong has been 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.

"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.