News Release

By JAN MCCOLM
UNC School of Medicine

CHAPEL HILL -- A newly refurbished structural biology facility at the University of North Carolina at Chapel Hill’s School of Medicine is enhancing research into protein structure and function.

The R.L. Juliano Structural Bioinformatics Core Facility honors Dr. Rudy Juliano, professor of pharmacology and former department chair.

"Structural biology is an important area that allows us a better understanding of proteins that are involved in the body’s responses to drugs," Juliano said.

Proteins are produced from genes as simple unfolded amino acid chains, but almost immediately fold themselves into a three-dimensional structure that creates the active interfaces required for the protein to perform its function.

An incorrectly folded protein may lead to diseases such as Alzheimer’s. Thus, knowledge of the folded structure of a protein is essential to understanding its function in health and disease, Juliano said.

Having begun in 1997 with five computers and a room nicknamed "the closet," the new core facility is nearly three times its former space, allowing room for nine computers, audiovisual facilities and a conference area.

"Part of my goal in supporting the facility is to make this kind of resource available to people who aren’t themselves trained as structural biologists," said Dr. Gary L. Johnson, professor of pharmacology and department chair.

Johnson’s research into hemorrhagic stroke uses the facility to study mutations in a group of recently discovered proteins. Mutations lead to changes in protein structures, which influence their folding, and this may alter a person’s susceptibility to stroke, Johnson said.

Knowledge of protein structure also is useful in drug design. Knowing the shape of the target protein makes it possible to search a database for molecules that will interact with it, said Dr. Brenda Temple, the core facility’s director.

"We can narrow the field of potential drugs, thus dramatically speeding up the process of drug discovery," Temple added.

One of the biggest benefits may come from genome research, Temple said. Inferring a simple protein sequence from a gene is a relatively easy process, but a facility such as UNC’s core facility is necessary to translate that into a functional protein, she added.

"We try predict the protein structure based on the closest experimental structures," Temple said, adding that sophisticated software algorithms then enable modeling of the unknown protein’s three-dimensional structure.

"We can help view protein structures, find the active sites, and we can in some cases help predict how a mutation may explain a result," Temple said.

Funding for the core facility was provided by a number of UNC sources: the departments of biochemistry and biophysics, cell and developmental biology, pharmacology, microbiology and immunology; the Program in Molecular Biology and Biotechnology; Academic Technology and Networks; the School of Medicine’s Office of the Dean; and UNC Lineberger Comprehensive Cancer Center.

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Note: Contact Temple at (919) 843-9399 or btemple@med.unc.edu.

School of Medicine contact: Les Lang, (919) 843-9687 or llang@med.unc.edu