1/20/2011

Brewer Receives 5-year NSF Grant

  • http-blogs-fandm-edu-wp-content-blogs-dir-29-files-2012-04-sbrewer-jpg Scott Brewer, assistant professor of chemistry  

The calendar may have switched to 2011, but the good news keeps rolling in for Scott Brewer.

Brewer, assistant professor of chemistry, has received a five-year, $403,115 CAREER grant from the National Science Foundation to support his project, “Probing Protein Folding Using Site-Specifically Encoded Unnatural Amino Acids.” It is the second major grant for Brewer in the past eight months. Along with Ed Fenlon, associate professor of chemistry, he received a three-year, $195,895 grant from the National Institutes of Health last spring.

The NSF’s CAREER program supports junior faculty who exemplify the role of teacher-scholars through the integration of teaching and research. Brewer joins Andrea Lommen, associate professor of astronomy, and Ryan Mehl, associate professor of chemistry, as recipients of a CAREER grant at Franklin & Marshall College.

To apply for a CAREER grant, professors must propose a project that contains both research and educational components. A portion of Brewer’s funding will allow F&M students to gain research experience. “This research experience plays a significant role in undergraduate education, as I experienced myself,” Brewer says. Brewer will also incorporate aspects of the research into physical chemistry courses.

Brewer will use the grant to explore the folding and unfolding of proteins, an active area of research due in part to the connection between protein misfolding and diseases such as Alzheimer’s, Parkinson’s and Huntington’s disease.

“Central to this research is understanding how a protein folds into its three-dimensional structure,” Brewer says.

A major difficulty in the study of protein folding is probing local environments without disturbing the structure of the protein. Consequently, Brewer’s research will focus on the synthesis, characterization and application of chemically modified amino acids to serve as sensitive spectroscopic probes of local protein structure and dynamics in a minimally invasive manner.

The chemically modified amino acids will be coupled with a number of spectroscopic techniques to measure structural changes associated with protein folding. This research methodology will also be applied to the study of protein misfolding, which is linked to a number of diseases.

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