Sup35 fibers

Sup35 Prions

 

Life demands that proteins fold into elaborate structures to perform the overwhelming majority of biological functions. We investigate how components of the proteostasis network enable cells to achieve successful protein folding. In particular, we seek to understand how cells prevent, reverse, or even promote the formation of diverse misfolded conformers, encompassing: prions, amyloids, fibrillar structures, amorphous aggregates and toxic soluble oligomers.

Hsp104new

The Protein Disaggregase, Hsp104
(Surface view colored by cylindrical radius)

click to videos of Hsp104

 

Our research program has been recognized by several prestigious awards including an NIH Director’s New Innovator Award, an American Heart Association National Scientist Development Award, an Ellison Medical Foundation New Scholar in Aging Award, a Bill and Melinda Gates Grand Challenges Explorations Award, and a Michael S. Brown New Investigator Award, which recognizes emerging faculty investigators engaged in innovative discoveries.

 

Department of Biochemistry & Biophysics
Perelman School of Medicine at The University of Pennsylvania
804-805B Stellar-Chance Laboratories
422 Curie Boulevard
Philadelphia, PA 19104-6059

215-573-4256

 

twitter

 

origami

fold

Successful folding!




 
Department of Biochemistry & Biophysics
p3
University of Pennsylvania