Inter-helix distances in lysophospholipid micelle-bound alpha-synuclein from pulsed ESR measurements. Academic Article uri icon

Overview

abstract

  • We demonstrate the use of pulsed ESR spectroscopy to measure intramolecular distances in the Parkinson's disease-associated protein alpha-synuclein bound to detergent and lysophospholipid micelles. We show that the inter-helical separation between the two helices formed upon binding to micelles is dependent on micelle composition, with micelles formed from longer acyl chains leading to an increased splaying of the two helices. Our data suggest that the topology of alpha-synuclein is not strongly constrained by the linker region between the two helices and instead depends on the geometry of the surface to which the protein is bound.

publication date

  • August 9, 2006

Research

keywords

  • Electron Spin Resonance Spectroscopy
  • Lysophospholipids
  • Micelles
  • alpha-Synuclein

Identity

Scopus Document Identifier

  • 33746894560

Digital Object Identifier (DOI)

  • 10.1021/ja063122l

PubMed ID

  • 16881616

Additional Document Info

volume

  • 128

issue

  • 31