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

Eyal Simonovsky; Henryk Kozlowski; Yifat Miller

doi:https://doi.org/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

Access to Document

https://doi.org/10.1039/c5ra15385a

Cite this

@article{276b742c2e764a56bcc67c7ed54c8452,

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",

month = dec,

day = "1",

doi = "https://doi.org/10.1039/c5ra15385a",

language = "American English",

volume = "5",

pages = "104551--104555",

journal = "RSC Advances",

issn = "2046-2069",

publisher = "Royal Society of Chemistry",

number = "126",

}

TY - JOUR

T1 - Termini capping of metal-poly-His peptide complexes induces the formation of α-helix

AU - Simonovsky, Eyal

AU - Kozlowski, Henryk

AU - Miller, Yifat

PY - 2015/12/1

Y1 - 2015/12/1

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.

UR - http://www.scopus.com/inward/record.url?scp=84950103932&partnerID=8YFLogxK

U2 - https://doi.org/10.1039/c5ra15385a

DO - https://doi.org/10.1039/c5ra15385a

M3 - Article

SN - 2046-2069

VL - 5

SP - 104551

EP - 104555

JO - RSC Advances

JF - RSC Advances

IS - 126

ER -

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

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this