Folded peptides have proven to be a fertile area for discovery of catalysts for reactions in organic synthesis. Both combinatorial chemistry and rational design have fueled these discoveries. In both lines of research, mechanistic studies following the discovery of selective reactions have led to structural information that has stimulated attempts to correlate peptide structure and the relay of stereochemical information. Thus, key elements of the design of peptide-based catalysts include the identification of catalytically competent functional groups and their incorporation into three-dimensional structures that provide an appropriate chiral environment. Of note, turns, helices, nonobvious folds, and still undetermined secondary structures characterize the structural and functionally diverse motifs that enable peptide-catalyzed asymmetric reactions to occur. © 2005 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 84: 38–47, 2006
This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at email@example.com
If you can't find a tool you're looking for, please click the link at the top of the page to "Go to old article view". Alternatively, view our Knowledge Base articles for additional help. Your feedback is important to us, so please let us know if you have comments or ideas for improvement.