These authors contributed equally.
Detection and Analysis of Chimeric Tertiary Structures by Backbone Thioester Exchange: Packing of an α Helix against an α/β-Peptide Helix†
Article first published online: 3 DEC 2009
Copyright © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 49, Issue 2, pages 368–371, January 8, 2010
How to Cite
Price, Joshua L., Hadley, Erik B., Steinkruger, Jay D. and Gellman, Samuel H. (2010), Detection and Analysis of Chimeric Tertiary Structures by Backbone Thioester Exchange: Packing of an α Helix against an α/β-Peptide Helix. Angew. Chem. Int. Ed., 49: 368–371. doi: 10.1002/anie.200904714
This research was supported by the NIH Grant GM-61238. J.L.P. was supported in part by an NIH Chemical Biology Training Grant (T32 GM008505). We thank Dr. Darrell McCaslin for assistance with AU experiments, and Peptech for providing β3-amino acids at a discounted price.
- Issue published online: 28 DEC 2009
- Article first published online: 3 DEC 2009
- Manuscript Received: 24 AUG 2009
- NIH. Grant Numbers: GM-61238, T32 GM008505
- protein folding;
Backbone thioester exchange is used to explore a fundamental type of protein–foldamer packing motif, the association of an α helix and an α/β-peptide foldameric helix, which is analogous to an antiparallel coiled-coil tertiary structure in a pure α-residue backbone. Side-chain packing preferences at this chimeric tertiary interface are comparable to those that determine pairing propensities among antiparallel α helices.