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- Title
Titelbild: Crystal Structure and NMR of an α,δ‐Peptide Foldamer Helix Shows Side‐Chains are Well Placed for Bifunctional Catalysis: Application as a Minimalist Aldolase Mimic (Angew. Chem. 36/2023).
- Authors
Lin, Qi; Lan, Hao; Ma, Chunmiao; Stendall, Ryan T.; Shankland, Kenneth; Musgrave, Rebecca A.; Horton, Peter N.; Baldauf, Carsten; Hofmann, Hans‐Jörg; Butts, Craig P.; Müller, Manuel M.; Cobb, Alexander J. A.
- Abstract
The stability of the helix and the modularity of the system (represented by the jigsaw pieces) means that different -amino acids can be used whilst maintaining the same helix type. Keywords: catalysis; peptidic foldamers; peptides; aldolase; helical conformation EN catalysis peptidic foldamers peptides aldolase helical conformation 1 1 1 08/31/23 20230904 NES 230904 B A helical catalyst b that is constructed from - and -amino acids: In their Research Article (e202305326), Alexander J. A. Cobb et al. present a foldamer helix whereby the catalytic functionalities are positioned in such a way that they can be exploited for bifunctional catalysis. The stability of the helix and the modularity of the system (represented by the jigsaw pieces) means that different -amino acids can be used whilst maintaining the same helix type.
- Subjects
BIFUNCTIONAL catalysis; LUMINOPHORES; PHOTOTHERMAL conversion; GOLDEN ratio; COLLOIDAL stability
- Publication
Angewandte Chemie, 2023, Vol 135, Issue 36, p1
- ISSN
0044-8249
- Publication type
Article
- DOI
10.1002/ange.202309523