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Jacob's Project Page - RISE summer 2004 |
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Intern: Jacob Koskimaki, University of Utah
Mentor: Emin Oroudjev
Faculty Supervisor: Helen Hansma
Department: Physics |
COMPARATIVE FORCE SPECTROSCOPY OF GLUTEN: HOW NONPOLAR AMINO ACID SIDE CHAINS CONTRIBUTE TO THE PROTEIN’S VISCOELASTIC NATURE
Gluten, a wheat storage protein fraction, is composed of subfractions
including glutenins and gliadins. These proteins contain significant amounts of
nonpolar amino acids, and are not readily dissolved in water due to their
hydrophobic nature. It has been found that a number of of these subproteins are
organized into a cross-linked network through the interaction of disulfide bonds.
Yet despite significant research efforts, the structural organization of individual
proteins and the corresponding network they form is still largely unknown.
Atomic force spectroscopy has proven to be one of the best methods of choice
for studying the physical and mechanical properties of single molecules, and
their organization in corresponding mesostructures. This technique can help
deduce how the largely nonpolar amino acid side chains of gluten contribute to
its viscoelastic nature. Understanding the protein’s viscoelasticity is
important for the utilization of wheat gluten in the food industry and some
technical applications.
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