Amie K. Boal
Department of Biochemistry and Molecular Biology and Chemistry
Pennsylvania State University
326 Chemistry Building, University Park, PA 16802
2014 Searle Scholar
Using metalloenzymes to facilitate new chemistry
Nature relies on the potent reactivity of metalloenzyme active sites to catalyze some of its most challenging chemical transformations. My research group uses X-ray crystallographic methods to understand the molecular basis for reactivity and substrate specificity in metalloproteins. We are particularly interested in systems for which the substrate is another macromolecule containing a large number of chemically and structurally similar sites. Structural characterization of these systems has the potential to offer unprecedented insight into target recognition and positioning in the active site, a particularly challenging scenario when the substrate is a large protein or structured nucleic acid. Our current efforts are focused on characterizing the structures of metalloenzymes that target RNA and other proteins, conformationally plastic substrates capable of adopting complex secondary or tertiary motifs. We ultimately aim to apply the knowledge gained in structural characterization of these systems to more effective exploitation of the technological potential of metalloenzymes, opportunities that are increasingly evident in the identification of these proteins as critical components in microbial biosynthetic and metabolic pathways.
|SITE MAP CONTACT US||© COPYRIGHT 2017 KINSHIP FOUNDATION. ALL RIGHTS RESERVED.|