12/10‐Helix in Mixed β‐Peptides Alternating Bicyclic and Acyclic β‐Amino Acids: Probing the Relationship between Bicyclic Side Chain and Helix Stability
Author:
Affiliation:
1. Institut des Biomolécules Max Mousseron (IBMM) UMR 5247CNRS-Université Montpellier-ENSCM 34093 Montpellier cedex 5 France
2. CRM2UMR 7063 CNRS Université de Lorraine Boulevard des Aiguilletes 54506 Vandoeuvre-lès-Nancy Cedex France
Publisher
Wiley
Subject
General Chemistry,Catalysis,Organic Chemistry
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/chem.201804404
Reference82 articles.
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2. Probing the Helical Secondary Structure of Short-Chain ?-Peptides
3. β-Peptides: a surprise at every turn
4. ‘Mixed’ β-peptides: A unique helical secondary structure in solution. Preliminary communication
5. ?2- and ?3-Peptides with Proteinaceous Side Chains: Synthesis and solution structures of constitutional isomers, a novel helical secondary structure and the influence of solvation and hydrophobic interactions on folding
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2. 6‐Strand to Stable 10/12 Helix Conformational Switch by Incorporating Flexible β‐hGly in the Homooligomers of Camphor Derived β‐Amino Acid: NMR and X‐Ray Crystallographic Evidence;Angewandte Chemie;2024-04-05
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