Can Helical Peptides Unwind One Turn at a Time? - Controlled Conformational Transitions in α,β2,3-Hybrid Peptides
Author:
Publisher
Wiley
Subject
General Chemistry,Catalysis,Organic Chemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1002/chem.201501198/fullpdf
Reference54 articles.
1. β-Peptide Foldamers: Robust Helix Formation in a New Family of β-Amino Acid Oligomers
2. Antiparallel Sheet Formation in β-Peptide Foldamers: Effects of β-Amino Acid Substitution on Conformational Preference1
3. ?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
4. Design of Secondary Structures in Unnatural Peptides: Stable Helical γ-Tetra-, Hexa-, and Octapeptides and Consequences of α-Substitution
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