Natural polypeptide scaffolds: β-sheets, β-turns, and β-hairpins
✍ Scribed by Kenneth S. Rotondi; Lila M. Gierasch
- Book ID
- 102760721
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2006
- Tongue
- English
- Weight
- 530 KB
- Volume
- 84
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
This paper provides an introduction to fundamental conformational states of polypeptides in the β‐region of φ,ψ space, in which the backbone is extended near to its maximal length, and to more complex architectures in which extended segments are linked by turns and loops. There are several variants on these conformations, and they comprise versatile scaffolds for presentation of side chains and backbone amides for molecular recognition and designed catalysts. In addition, the geometry of these fundamental folds can be readily mimicked in peptidomimetics. © 2005 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 84: 13–22, 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 protected]
📜 SIMILAR VOLUMES
## Abstract Designed octapeptides Boc‐Leu‐Val‐Val‐Aib‐^D^Xxx‐Leu‐Val‐Val‐OMe (^D^Xxx = ^D^Ala, 3a;^D^Val, 3c and ^D^Pro, 5a) and Boc‐Leu‐Phe‐Val‐Aib‐^D^Ala‐Leu‐Phe‐Val‐OMe (3b) have been investigated to construct models of a stable type I′ β‐turn nucleated hairpin and to generate systems for invest