Detection of transient interchain interactions in the intrinsically disordered protein α-synuclein by NMR paramagnetic relaxation enhancement

Kuen Phon Wu, Jean Baum

Research output: Contribution to journalArticlepeer-review

66 Scopus citations

Abstract

NMR paramagnetic relaxation enhancement experiments were applied to the intrinsically disordered protein α-synuclein, the primary protein in Parkinson's disease, to directly characterize transient intermolecular complexes at neutral and low pH. At neutral pH, we observed weak N- to C-terminal interchain contacts driven by electrostatic interactions, while at low pH, the C- to C-terminal interchain interactions are significantly stronger and driven by hydrophobic contacts. Characterization of these first interchain interactions will provide fundamental insight into the mechanism of amyloid formation.

Original languageEnglish (US)
Pages (from-to)5546-5547
Number of pages2
JournalJournal of the American Chemical Society
Volume132
Issue number16
DOIs
StatePublished - Apr 28 2010

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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