title: Allosteric stabilization of the amyloid-β peptide hairpin by the fluctuating N-terminal.
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.
authors.affiliation: School of Chemistry, Dalian University of Technology, Dalian, China.
authors.forename: Liang
authors.initials: L
authors.lastname: Xu
authors.forename: Ruth
authors.initials: R
authors.lastname: Nussinov
authors.forename: Buyong
authors.initials: B
authors.lastname: Ma
mesh_terms: D000494:Allosteric Regulation; D058227:Amyloidogenic Proteins / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*
chemical_list: D058227:Amyloidogenic Proteins; D010455:Peptides