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

Liang Xu; Ruth Nussinov; Buyong Ma

doi:10.1039/c5cc08107f

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

Liang Xu, Ruth Nussinov, Buyong Ma^*

^*Corresponding author for this work

Human Molecular Genetics Biochemistry

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

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.

Original language	English
Pages (from-to)	1733-1736
Number of pages	4
Journal	Chemical Communications
Volume	52
Issue number	8
DOIs	https://doi.org/10.1039/c5cc08107f
State	Published - 2016

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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.",

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PY - 2016

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AB - 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.

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

Abstract

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