Preferred conformation of the terminally blocked (Aib)10 homo-oligopeptide: A long, regular 310-helix-Reference-Cited by-同舟云学术

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Preferred conformation of the terminally blocked (Aib)10 homo-oligopeptide: A long, regular 310-helix

Published:1991-01 Issue:1 Volume:31 Page:129-138
ISSN:0006-3525
Container-title:Biopolymers
language:en
Short-container-title:Biopolymers

Author:

Toniolo Claudio,Crisma Marco,Bonora Gian Maria,Benedetti Ettore,Dl Blasio Benedetto,Pavone Vincenzo,Pedone Carlo,Santini Antonello

Publisher

Wiley

Subject

Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics

Reference49 articles.

1. The longest, regular polypeptide 310 helix at atomic resolution

2. Preferred conformations of peptides containing ?,?-disubstituted ?-amino acids

3. The Stereochemistry of Peptides Containing α-Aminoisobutyric Aci

4. Structural Versatility of Homo-peptides from Cα,α-dialkylated Glycines

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1. Redox‐Triggered Reversible Switching between Dynamic and Quasi‐static α‐Helical Peptides;Chemistry – A European Journal;2024-09-10

2. Revisiting 310-helices: biological relevance, mimetics and applications;Exploration of Drug Science;2024-02-01

3. Stapling strategy for slowing helicity interconversion of α-helical peptides and isolating chiral auxiliary-free one-handed forms;Nature Communications;2023-10-26

4. Helices in Peptides Containing Differentially Geminally Di‐substituted γ Amino Acid Residues;ChemistrySelect;2023-07-03

5. Secondary Structures in Synthetic Poly(Amino Acids): Homo‐ and Copolymers of Poly(Aib), Poly(Glu), and Poly(Asp);Macromolecular Bioscience;2023-01-20

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