An Unusual Interstrand H-Bond Stabilizes the Heteroassembly of Helical αβγ-Chimeras with Natural Peptides-Reference-Cited by-同舟云学术

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An Unusual Interstrand H-Bond Stabilizes the Heteroassembly of Helical αβγ-Chimeras with Natural Peptides

Published:2014-01-10 Issue:3 Volume:9 Page:613-616
ISSN:1554-8929
Container-title:ACS Chemical Biology
language:en
Short-container-title:ACS Chem. Biol.

Author:

Nyakatura Elisabeth K.¹,Rezaei Araghi Raheleh¹,Mortier Jérémie¹²,Wieczorek Sebastian¹,Baldauf Carsten³,Wolber Gerhard²,Koksch Beate¹

Affiliation:

1. Institute of Chemistry and Biochemistry, Freie Universität Berlin, Takustraße 3, 14195 Berlin, Germany

2. Institute of Pharmacy, Freie Universität Berlin, Königin-Luisestrasse 2+4, 14194 Berlin, Germany

3. Fritz Haber Institute, Faradayweg 4-6, 14195 Berlin, Germany

Publisher

American Chemical Society (ACS)

Subject

Molecular Medicine,General Medicine,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/cb4007979

Reference32 articles.

1. β-Peptides: Synthesis by Arndt-Eistert homologation with concomitant peptide coupling. Structure determination by NMR and CD spectroscopy and by X-ray crystallography. Helical secondary structure of a β-hexapeptide in solution and its stability towards pe

2. Foldamers: A Manifesto

3. β-Peptides: From Structure to Function

4. A Field Guide to Foldamers

5. Structural Chemistry of Peptides Containing Backbone Expanded Amino Acid Residues: Conformational Features of β, γ, and Hybrid Peptides

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4. Computational close up on protein-protein interactions: how to unravel the invisible using molecular dynamics simulations?;Wiley Interdisciplinary Reviews: Computational Molecular Science;2015-07-27

5. Makromolekulare Chemie 2014;Nachrichten aus der Chemie;2015-03

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