Lipid Bilayer Interactions of Amyloidogenic N-Terminal Fragment of Apolipoprotein A-I Probed by Förster Resonance Energy Transfer and Molecular Dynamics Simulations.

Abstract excerpt

The effects of one of the amyloidogenic mutations of apolipoprotein A-I (apoA-I), G26R, on the thermal stability, structural dynamics and lipid-associating properties of the 1-83 N-terminal fragment of apoA-I (A83) have been investigated using the Förster resonance energy transfer (FRET) and molecular dynamics (MD) simulation. The measurements of FRET between the tryptophan residues of the single Trp variants of...

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