ORGN 677 |
| We report the structural and functional characterizations of a series of self-assembling coiled-coil peptides that have been designed to mimic the intermodular aminoacyl transfer function of nonribosomal peptide synthetases (NRPS). In particular, we will emphasize the role of active site residues and arrangements in promoting efficient aminoacyl transfer in neutral aqueous solutions (rate enhancements of more than 5 orders of magnitude) and how they can be used to control selective activation of aminoacyl donor and acceptor units. We will conclude this lecture by describing the design and functional characterizations of a catalytic diketopiperazine synthetase (DKPS) mimic.
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Lipids, Nucleotides, and Mimetics
1:00 PM-4:40 PM, Wednesday, 13 September 2006 Moscone Center -- Room 131, Oral
Division of Organic Chemistry |
