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

Eyal Simonovsky; Henryk Kozlowski; Yifat Miller

doi:10.1039/c5ra15385a

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

Eyal Simonovsky, Henryk Kozlowski, Yifat Miller

Ben-Gurion University of the Negev

Research output: Contribution to journal › Article › peer-review

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.

Original language	American English
Pages (from-to)	104551-104555
Number of pages	5
Journal	RSC Advances
Volume	5
Issue number	126
DOIs	https://doi.org/10.1039/c5ra15385a
State	Published - 1 Dec 2015

All Science Journal Classification (ASJC) codes

General Chemistry
General Chemical Engineering

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title = "Termini capping of metal-poly-His peptide complexes induces the formation of α-helix",

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.",

author = "Eyal Simonovsky and Henryk Kozlowski and Yifat Miller",

note = "Publisher Copyright: {\textcopyright} The Royal Society of Chemistry.",

year = "2015",

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AU - Simonovsky, Eyal

AU - Kozlowski, Henryk

AU - Miller, Yifat

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N2 - 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.

AB - 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.

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U2 - 10.1039/c5ra15385a

DO - 10.1039/c5ra15385a

M3 - Article

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VL - 5

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JO - RSC Advances

JF - RSC Advances

IS - 126

ER -

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

Abstract

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