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Issue 8, 2016
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Allosteric stabilization of the amyloid-β peptide hairpin by the fluctuating N-terminal

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Abstract

Immobilized ions modulate nearby hydrophobic interactions and influence molecular recognition and self-assembly. We simulated disulfide bond-locked double mutants (L17C/L34C) and observed allosteric modulation of the peptide's intra-molecular interactions by the N-terminal tail. We revealed that the non-contacting charged N-terminal residues help the transfer of entropy to the surrounding solvation shell and stabilizing β-hairpin.

Graphical abstract: Allosteric stabilization of the amyloid-β peptide hairpin by the fluctuating N-terminal

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Publication details

The article was received on 28 Sep 2015, accepted on 02 Dec 2015 and first published on 02 Dec 2015


Article type: Communication
DOI: 10.1039/C5CC08107F
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Citation: Chem. Commun., 2016,52, 1733-1736
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    Allosteric stabilization of the amyloid-β peptide hairpin by the fluctuating N-terminal

    L. Xu, R. Nussinov and B. Ma, Chem. Commun., 2016, 52, 1733
    DOI: 10.1039/C5CC08107F

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