Research Focus | Protein Engineering and Synthetic Biology
Inspired by nature, we develop new methods to build biological parts (proteins, peptides, and nucleic acids) and systems with designed properties and predictable behaviors. Operating at the interface of biology, biochemistry, and bioengineering we focus on how the information contained at the sequence level leads to various properties at the molecular level and how this knowledge can be used to engineer molecules with novel characteristics. We repurpose biological cells as factories allowing simple large-scale low-cost manufacturing of complex macromolecules. This is an area with immense potential to address many challenges facing our world such as reducing disease burden, addressing climate change, tackling pollution, and enabling a sustainable supply of food and energy.
Major problems we are trying to solve:
- New therapeutic biologics and delivery systems.
- Design and discovery of functional proteins and peptides.
- Low-cost large-scale biosensing.
- Predictive models of sequence-function relationships.
Participating Research Groups
Within the Knight Campus and in the UO’s Department of Chemistry and Biochemistry and the Institute of Molecular Biology, faculty share an interest in discovering how natural systems carry out specific functions at the molecular scale and how this knowledge can be used to develop new technologies. Participating research groups have expertise in:
- Protein engineering (Hettiaratchi, Hosseinzadeh, Plesa).
- Computational methods (Cresko, Hosseinzadeh).
- RNA based systems (DeRose, Garcia).
- Biosensing (Guillemin, Hosseinzadeh, Plesa).
Bioengineering Program Faculty — Protein Engineering and Synthetic Biology
EXPLORE OUR BIOENGINEERING RESEARCH GROUPS
UO Collaborators
Bill Cresko
Department of Biology
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Vickie DeRose
Department of Chemistry and Biochemistry
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David Garcia
Department of Biology
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Mike Harms
Department of Chemistry and Biochemistry
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Ken-ichi Noma
Department of Biology
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James Prell
Department of Chemistry and Biochemistry
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