Patricia Soto  

Associate Professor of Physics
Creighton University 
Omaha, Nebraska, USA


Funding: Nebraska INBRE-NIH, Nebraska EPSCoR - NSFDr. George F. Haddix Presidential Faculty Research Fund, summer CURAS award, summer graduate fellowship.

Key words:

Science topics: protein conformational dynamics, pathological protein folding, prion proteins
Technique: computational statistical mechanics, biomolecular modeling, molecular dynamics simulations, molecular docking, continuum electrostatics, normal mode analysis, structural bioinformatics, residue network analysis.

What do we do?

Our quest is to establish a molecular-level mechanism that explains amyloid proteins misfolding and pathological seeding. 

We focus on fatal amyloid diseases, such as prion diseases, Alzheimer's disease, and immunoglobin light chain (AL) amyloidosis.

The outcome of our research will aid in the identification of early diagnostic markers and the design of targeted therapeutic tools against amyloid diseases.

For the non-specialist:

Alzheimer’s disease. Mad Cow disease. CJ disease. Parkinson’s disease. Huntington’s disease. All these apparently unrelated amyloid diseases result when proteins do not attain the shape they should have. What are proteins? Proteins are the biological nanomachines that perform specific functions to ensure the well being of every living cell. How do proteins attain the right shape? Our research uses physical sciences and high-performance computing methods to advance our understanding of the process of protein folding (or how proteins attain the right shape). The link between misfolded proteins (or proteins with the wrong shape) and amyloid diseases is addressed together with potential avenues for the rational design of diagnostic tools and therapeutics. Interestingly enough, similar physical principles may lay foundations for the design of bio-inspired nanoassemblies.

Students working in our group are exposed to current exciting challenges in the fields of biomolecular sciences and biotechnology and have the chance to be part of a world wide computational biophysics community.
What to expect from the research experience in our group? 

  • Advance the field of amyloid protein biophysics: Discover the structural mechanism by which amyloid proteins, hallmark of prion diseases and Alzheimer's disease among others, misfold and seed pathological oligomers.
  • Belong to a joyful and inclusive community of undergraduate and master's students engaged in authentic interdisciplinary research: Since 2008, about ~40 students from ~10 different academic programs have been active members of our group.
  • Strengthen your communication and networking skills: Students in our group present their research outcomes at local, regional and national venues. 
  • Make informed decisions for your path after graduation: Our students go into graduate school, medical school, dental school, and the knowledge industry workforce among others.