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 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. It’s 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 … 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, it’s through the approach (research) I’ll
discover other things that will help me figure out what’s
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 master’s degree in biochemistry at
the University of Chicago, and a Ph.D. in
biochemistry-biophysics at Oregon State University.
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