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Hydrogen exchange of monomeric α-synuclein shows unfolded structure persists at physiological temperature and is independent of molecular crowding in Escherichia coli

  1. Robyn L. Croke1,
  2. Christine O. Sallum1,
  3. Emma Watson1,
  4. Eric D. Watt2,
  5. Andrei T. Alexandrescu1,*

Article first published online: 2 JAN 2009

DOI: 10.1110/ps.033803.107

Issue

Protein Science

Protein Science

Volume 17, Issue 8, pages 1434–1445, August 2008

Additional Information

How to Cite

Croke, R. L., Sallum, C. O., Watson, E., Watt, E. D. and Alexandrescu, A. T. (2008), Hydrogen exchange of monomeric α-synuclein shows unfolded structure persists at physiological temperature and is independent of molecular crowding in Escherichia coli. Protein Science, 17: 1434–1445. doi: 10.1110/ps.033803.107

Author Information

  1. 1

    Department of Molecular and Cell Biology, University of Connecticut, Storrs, Connecticut 06269-3125, USA

  2. 2

    Department of Chemistry, Yale University, New Haven, Connecticut 06520, USA

*Department of Molecular and Cell Biology, University of Connecticut, 91 North Eagleville Road, U-3125, Storrs, CT 06269-3125, USA; fax: (860) 486-4331.

Publication History

  1. Issue published online: 2 JAN 2009
  2. Article first published online: 2 JAN 2009
  3. Manuscript Accepted: 12 MAY 2008
  4. Manuscript Revised: 7 MAY 2008
  5. Manuscript Received: 3 DEC 2007

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