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      Conformational properties of alpha-synuclein in its free and lipid-associated states.

      1 , , ,
      Journal of molecular biology
      Elsevier BV

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          Abstract

          alpha-Synuclein (alphaS) is a presynaptic terminal protein that is believed to play an important role in the pathogenesis of Parkinson's disease (PD). We have used NMR spectroscopy to characterize the conformational properties of alphaS in solution as a free monomer and when bound to lipid vesicles and lipid-mimetic detergent micelles. Free wild-type alphaS is largely unfolded in solution, but exhibits a region with a preference for helical conformations that may be important in the aggregation of alphaS into fibrils. The N-terminal region of alphaS binds to synthetic lipid vesicles and detergent micelles in vitro and adopts a highly helical conformation, consistent with predictions based on sequence analysis. The C-terminal part of the protein does not associate with either vesicles or micelles, remaining free and unfolded. These results suggest that one function of alphaS may be to tether as of yet unidentified partners to lipid surfaces via interactions with its C-terminal tail.

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          Author and article information

          Journal
          J Mol Biol
          Journal of molecular biology
          Elsevier BV
          0022-2836
          0022-2836
          Apr 06 2001
          : 307
          : 4
          Affiliations
          [1 ] Department of Biochemistry and Program in Structural Biology, Weill Medical College of Cornell University, New York, NY, 10021, USA. dae2005@mail.med.cornell.edu
          Article
          S0022-2836(01)94538-3
          10.1006/jmbi.2001.4538
          11286556
          08e76803-be42-4f4e-86d5-50c888400a44
          Copyright 2001 Academic Press.
          History

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