Bryan F. Shaw, Ph.D.

Education

• Post-doctoral fellow, Harvard University 2006-2010
• Ph.D., Inorganic Chemistry, University of California, Los Angeles, Dec. 2005
• B.S., Biochemistry and Biophysics, Washington State University, May, 1999

Appointed to Faculty at Baylor University, August 2010

Research

Research in the Shaw laboratory is a mix of bio-inorganic chemistry, protein biophysics-with a focus on protein misfolding and amyotrophic lateral sclerosis-and a dash of medicinal chemistry and proteomics.

The Shaw research group is engaged in two different types of outreach activities to children and young adults who are visually impaired. The first project is utilizing rapid prototyping (3D printing) to generate atomically accurate models of proteins from the X-ray crystal structures that are deposited in the Protein Data Bank (see examples of hemoglobin and calmodulin on homepage). These models are being used in local school districts throughout central Texas to teach blind high school students about the dynamic nature of protein structure (specifically, protein allostery). A second outreach project is more technical and is developing tools to improve a parent's ability to detect retinoblastoma with consumer-based digital photography. Retinoblastoma is a devastating eye cancer that affects children under the age of five years. Retinoblastoma strikes ~8,000 children throughout the world each year and claims the lives of ~4000. The cardinal symptom of retinoblastoma is the appearance of leukocoria ("white eye") in a recreational digital photograph. An example of a leukocoria in a photograph of a child with retinoblastoma is shown below. Unfortunately, by the time a parent begins to notice leukocoria, the cancer is so advanced that the eye is often enucleated.

The Shaw Research Group

Bioanalytical Chemistry

Research in the Shaw Laboratory occurs at the crossroads of chemistry, structural biology, proteomics and biophysics. One of our primary aims is to understand how changes in the electrostatic properties of a protein can accelerate its aggregation. The aggregation of certain proteins can cause human diseases such as amyotrophic lateral sclerosis. We intend to apply our work in protein biophysics and protein chemistry towards the development of new classes of small molecules that can inhibit the aggregation of proteins. Visit us at the lab's website to learn more about our research!