Dr. John C. Sherman’s research was recently featured on the inside cover of Chemistry – A European Journal. The article, “Conformationally Constrained Sequence Designs to Bias Monomer–Dimer Equilibriums in TASP Systems” was co-authored by Dr. Jon O. Freeman.
According to Dr. Sherman, his work demonstrates an ability to bias a synthetic protein toward either a monomer or a dimer via incorporation of either metal binding sites or disulfide bonds. He states that “our synthetic proteins are directed by templates (template-assembled synthetic proteins or TASPs), and are largely monomeric in solution. Recently, we reported the first crystal structure of a TASP (JACS 2009, p. 7421), which has a dimeric structure in the solid state. The present work shows that we can control the oligomeric state in solution.”
This research contributes to a general ability to control tertiary structure in both natural and synthetic proteins, and may be applicable in protein-protein interactions as well as in a number of diseases involving oligomerization including Huntington's, Parkinson's, and Creutzfeldt-Jackob disease.
The full article can be viewed online at: http://onlinelibrary.wiley.com/doi/10.1002/chem.201102171/abstract