| Research in the Baneyx laboratory intersects engineering, biology and nanotechnology. How proteins fold into intricate three-dimensional shapes - or why they sometimes fail to do so - has profound implications in medicine and biotechnology. We study the genetics, regulation and structure-function relationship of molecular chaperones, a class of proteins that help other polypeptides reach a correct conformation. We exploit this fundamental understanding to facilitate the production of recombinant proteins in a biologically active form, to build biosensors, and to explore the connection between protein (mis)folding and neurodegenerative diseases.
In the nanobiotechnology arena, we are interested in isolating and characterizing short peptides that bind to inorganic or synthetic compounds. We engineer these peptides within well-characterized protein "scaffolds" and use the resulting designer proteins to nucleate, organize and assemble nanostructured materials, with the aim of building systems and devices exhibiting superior mechanical or opto-electronic properties.
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| To display biological activity, newly synthesized proteins must fold into a precise three-dimensional conformation stabilized by hydrogen bonds, van der Waals interactions, hydrophobic interactions, salt bridges and disulfide bonds. Although all the information necessary for a protein to reach a correct structure is contained in its amino acid sequence, recombinant proteins of therapeutic or commercial interest are often unable to properly fold or reach a correct cellular location (e.g., the cell membrane) when expressed at high levels in bacteria or higher cells. The resulting misfolded proteins may either be degraded by cellular proteases or, more commonly, become sequestered as inclusion bodies which are insoluble proteinaceous aggregates refractile to light.
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