PhD, Postdoctoral Fellow, Fox Chase Cancer Center: Developmental Therapeutics Philadelphia
The ins and outs of charges in membrane proteins
I will describe my contributions to three membrane-protein science findings that span molecular biology, bioinformatics, and protein design.
Using charges to control inner membrane protein topology, it has been determined that inner membrane proteins remain topologically uncommitted until the very last residue has been synthesized.
It has been determined that there is a dramatic asymmetry in the charge distribution within outer membrane beta barrels. This asymmetry has important implications for understanding the mechanism of outer membrane protein insertion.
By devising a method of computational protein design using mostly van der Waals forces, peptides that bind to membrane proteins were produced. These peptides bound their targets with high specificity and affinity.