ORGN 350 |
| Proteins perform a wide range of complex functions in biological systems. Nearly all of these molecular operations require the polypeptide chain to adopt a compact and specific folding pattern, and understanding the origins of peptide folding preferences has been a long-term goal. One major contribution to this goal from peptide science has been the identification and characterization of model systems for protein substructures, such as alpha-helices, beta-turns and beta-sheets. Over the past 10-15 years, it has become increasingly popular to extrapolate from natural peptide systems to other types of folding oligo- and polyamides. Beta-peptides (oligomers of beta-amino acids) have been particularly widely studied. This lecture will cover folding rules that have been established for beta-peptides and for newer classes of heterogeneous oligomers containing both alpha- and beta-amino acid residues. Biological applications of these foldamers will be presented as well. |
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Ralph F. Hirschmann Award in Peptide Chemistry: Symposium in Honor of Samuel H. Gellman
1:15 PM-5:00 PM, Tuesday, March 27, 2007 McCormick Place Lakeside -- Room E451A/B, Level 4, Oral
Division of Organic Chemistry |