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Student research at BHSU receives $112,935 NSF grant

Undergraduate students at Black Hills State University will benefit from a $112,935 grant from the National Science Foundation (NSF) that will introduce them to pure research.

Dr. Mike Zehfus, assistant professor of chemistry at BHSU, wrote the grant to research the importance of the hydrogen bond in protein structure. Over the next three years, six undergraduate students will study hydrogen bonds by making model proteins with hydrogen bonds, then chemically remove specific hydrogen bonds to see how much the structure changes.

Not only is grant funding for this type of pure research highly competitive, but it is almost always reserved for graduate programs at major graduate research institutions.

"This is good run-of-the-mill research at the graduate level," said Zehfus. "This may be a first for this type of grant at Black Hills State. Itís rare or uncommon at the undergraduate level."

The BH chemistry professor cited several reasons why the grant application appealed to NSF: "they liked the undergraduate involvement; they liked the combination of theoretical chemistry, organic chemistry, and biochemistry; and they liked the use of techniques not normally found at the undergraduate level. It provides lots of exposure for our students."

The fact that the university has a circular dichroism machine that can monitor protein structure, helped to secure the grant, he said. Equipment like that is rare, even at large research institutions.

"It is now possible to determine how much helix is lost due to removal of the single hydrogen bond," said Zehfus.

His grant proposal outlines a series of experiments that will measure the strength of the backbone hydrogen bond in an alpha helix. He explained that proteins are long chains of amino acids that have the same backbone. The

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hydrogen bonds help hold it together and determine the overall structure.

"The whole idea is to chemically destroy one of these linkages by changing its chemistry Ö and then determine how much that weakens the overall helix," he said. "The key is changing chemistry of the peptide linkage itself."

Zehfus said, "Much work has been done to measure hydrogen bonding forces in amino acid sidechains, comparatively little work has been done with the main chain hydrogen bonds due to the difficulty in manipulating backbone-backbone interaction."

The BH chemistry professor said that at this time there is no direct commercial application for this type of research. It does, however, help in the fundamental understanding of how proteins work and what makes their structure.

As an end result, Zehfus hopes to have a number that measures the strength of the hydrogen bond. He did admit, however, that it is more about the pursuit of the number than determining an actual final figure.

"I may never actually get that number, itís through the approach (research) Iíll discover other things that will help me figure out whatís going on."

In pursuit of that elusive number, he and two BH students will spend each summer for the next three years building protein models and analyzing their structures with the circular dichroism machine. One student will also work part-time on the project during the academic year and several students will attend national science conferences with the chemistry professor.

Zehfus joined the BHSU science faculty two years ago after serving as an assistant professor in the College of Pharmacy at Ohio State University and as a visiting assistant professor in the department of chemistry at Ohio Northern University. He is a graduate of Ripon College, Ripon, Wisc., and earned a masterís degree in biochemistry at the University of Chicago, and a Ph.D. in biochemistry-biophysics at Oregon State University.