Monday, November 12, 2012 - Thursday, November 15, 2012
Location: 310 ICTAS-1
The Macromolecules and Interfaces Institute and the Fralin Life Science Institute at Virginia Tech are pleased to announce that David Tirrell, the Ross McCollum-William H. Corcoran Professor of Chemistry and Chemical Engineering and Director of the Beckman Institute at the California Institute of Technology, will be the Fralin-MII Visiting Scholar from Nov. 12-15.
- Lecture 1: Genetically Programmed Synthesis of Novel Macromolecules (Monday, Nov. 12, 310 ICTAS-I, 11:15 a.m.-12:15 p.m.): The first lecture will provide an overview of the use of molecular genetics to prepare novel macromolecules. The motivation for adopting this approach will be discussed, along with challenges in implementation. Use of the approach to control macromolecular assembly, to evolve proteins of novel composition, and to engineer proteins for therapeutic applications will be described. Results of recent clinical trials will be presented.
- Lecture 2: Proteins that Nature Never Made (Tuesday, Nov. 13, 310 ICTAS-I, 11:15 a.m.-12:15 p.m.) Macromolecular chemistry has traditionally been divided into two fields, with biochemists and biochemical engineers working on proteins and nucleic acids while polymer chemists and materials scientists have concerned themselves with synthetic polymers. These two classes of macromolecules are profoundly different from one another; proteins and nucleic acids are uniform, well folded, and evolvable, whereas polymers are heterogeneous and for the most part adopt random-coil conformations. These differences in molecular structure and behavior have led to striking differences in the ways in which natural and synthetic polymers are used-- largely for information storage and transfer in biology, and largely as materials in the technological world. This lecture will describe an ongoing attempt to bridge the gap between polymers and proteins by using artificial genes to direct the synthesis of artificial proteins in bacterial cells, and to combine the physical and informational properties of macromolecules.
- Lecture 3: Non-Canonical Amino Acids in the Interrogation of Cellular Protein Synthesis (Thursday, Nov. 15, 310 ICTAS-I, 11:15 a.m.-12:15 p.m.) Proteins can be rendered susceptible to bio-orthogonal chemistries through metabolic labeling with appropriately designed, non-canonical amino acids (ncAAs). In the simplest approach to metabolic labeling, an amino acid analog replaces, in whole or in part, one of the natural amino acids specified by the protein gene(s) of interest. This approach allows the ncAA to be introduced at a controlled rate into positions normally occupied by the natural amino acid residue. Because this approach permits labeling of proteins throughout the cell, it has enabled us to develop strategies to track cellular protein synthesis by tagging proteins with reactive ncAAs.
Contact: Lindsay Taylor Key
Email: ltkey@vt.edu
Website
View Full Calendar ->
