Allosteric stabilization of the amyloid-? peptide hairpin by the fluctuating N-terminal.
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ABSTRACT:
SUBMITTER: Xu L
PROVIDER: S-EPMC4720562 | biostudies-literature | 2016 Jan
REPOSITORIES: biostudies-literature
Publications
Allosteric stabilization of the amyloid-β peptide hairpin by the fluctuating N-terminal.
Xu Liang L Nussinov Ruth R Ma Buyong B
Chemical communications (Cambridge, England) 20151215 8
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. ...[more]
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