Issue 126, 2015
From the journal:

RSC Advances

Termini capping of metal-poly-His peptide complexes induces the formation of α-helix†

Eyal Simonovsky,ab   Henryk Kozlowski*c  and  Yifat Miller*ab  

* Corresponding authors

a Department of Chemistry, Ben-Gurion University of the Negev, Beer-Sheva 84105, Israel

b Ilse Katz Institute for Nanoscale Science and Technology, Beer-Sheva 84105, Israel
E-mail: ymiller@bgu.ac.il

c Faculty of Chemistry, University of Wroclaw, 50-383 Wroclaw, Poland
E-mail: henryk.kozlowski@chem.uni.wroc.pl

Abstract

An ensemble of structures of metal-hexa-histidine-tag capped and uncapped peptides has been studied using molecular dynamics simulations. The metal-binding peptides are polymorphic for both capped and uncapped peptides. The capping of the peptide termini promotes α-helical conformations that are induced by the metal binding sites.

Graphical abstract: Termini capping of metal-poly-His peptide complexes induces the formation of α-helix

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Article information

DOI
https://doi.org/10.1039/C5RA15385A
Article type
Communication
Submitted
02 Aug 2015
Accepted
30 Nov 2015
First published
01 Dec 2015
This article is Open Access
Creative Commons BY license

RSC Adv., 2015,5, 104551-104555

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Termini capping of metal-poly-His peptide complexes induces the formation of α-helix

E. Simonovsky, H. Kozlowski and Y. Miller, RSC Adv., 2015, 5, 104551 DOI: 10.1039/C5RA15385A

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