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

Liang Xu, Ruth Nussinov, Buyong Ma*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

24 Scopus citations

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 languageEnglish
Pages (from-to)1733-1736
Number of pages4
JournalChemical Communications
Volume52
Issue number8
DOIs
StatePublished - 2016

Funding

FundersFunder number
National Institutes of HealthHHSN261200800001E
National Cancer InstituteZIABC010441
Council for Chemical Research
China Scholarship CouncilCSC201306065001

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