Interruption of a 310-helix by a single Gly residue in a poly-Aib motif: A crystallographic study
Author:
Publisher
Wiley
Subject
Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics
Reference38 articles.
1. Structural characteristics of .alpha.-helical peptide molecules containing Aib residues
2. Controls exerted by the Aib residue: Helix formation and helix reversal This article is a US Government work and, as such, is in the public domain in the United States of America.
3. Control of peptide conformation by the Thorpe-Ingold effect (C?-tetrasubstitution)
4. Peptide design: Influence of a guest Aib-Pro segment on the stereochemistry of an Oligo-Val sequence?solution conformations and crystal structure of Boc-(Val)2-Aib-Pro-(Val)3-OMe
5. A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-Å resolution
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1. Revisiting 310-helices: biological relevance, mimetics and applications;Exploration of Drug Science;2024-02-01
2. A rationally engineered small antimicrobial peptide with potent antibacterial activity;Journal of Cellular Biochemistry;2023-11-22
3. Ambidexterity and Left-Handedness Induced by Geminally Disubstituted γ Amino Acid Residues in Chiral 310 Helices;ACS Omega;2023-09-21
4. De novo design of discrete, stable 310-helix peptide assemblies;Nature;2022-06-22
5. Constructing synthetic-protein assemblies from de novo designed 310 helices;2021-12-11
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