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Ariel's Project Page - RISE summer 2004 |
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Intern: Ariel Brumbaugh, University of Washington
Mentor: Jason Sagert
Faculty Supervisor: Herbert Waite
Department: Molecular Cellular and Developmental Biology |
SECONDARY STRUCTURE ANALYSIS OF A PROMINENT PROTEIN IN MUSSEL BYSSAL THREADS
As Marine mussels thrive attached to substrates along rocky intertidal
seashores where water velocities can reach as high as ten meters per second.
A key adaptation in the mussels’ survival in this high-energy environment is
their proteinacous holdfast known as the byssus. The byssus is a collection of
protein-rich threads which are excreted by the mussel and have a unique
combination of mechanical properties which have yet to be replicated in any
man-made material.
Some of those properties include: a high toughness, a large stiffness gradient
(ranging from rubber at one end of the fiber to nylon at the other) and the
ability to ‘self-heal’ after deformation. Through understanding the proteins
that function in the byssus, synthetic materials could be designed to mimic the
desired mechanical properties and therefore impact such ranging fields from
dentistry to cross-ocean shipping. A novel 56 kDa protein has been purified
and partially characterized and a portion of this protein has been recombinantly
expressed for analysis of secondary structure using circular dichroism and light
scattering techniques.
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