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Rotational orientation of monomers within a designed homo-oligomer transmembrane helical bundle

  1. Kathleen P. Howard1,*,
  2. Wei Liu2,
  3. Evan Crocker3,
  4. Vikas Nanda4,
  5. James Lear4,
  6. William F. Degrado4,
  7. Steven O. Smith2,*

Article first published online: 1 JAN 2009

DOI: 10.1110/ps.041110605

Issue

Protein Science

Protein Science

Volume 14, Issue 4, pages 1019–1024, April 2005

Additional Information

How to Cite

Howard, K. P., Liu, W., Crocker, E., Nanda, V., Lear, J., Degrado, W. F. and Smith, S. O. (2005), Rotational orientation of monomers within a designed homo-oligomer transmembrane helical bundle. Protein Science, 14: 1019–1024. doi: 10.1110/ps.041110605

Author Information

  1. 1

    Department of Chemistry, Swarthmore College, Swarthmore, Pennsylvania 19081, USA

  2. 2

    Department of Biochemistry and Cell Biology, Center for Structural Biology, Stony Brook University, Stony Brook, New York 11794-5115, USA

  3. 3

    Department of Physics and Astronomy, Stony Brook University, Stony Brook, New York 11794-5115, USA

  4. 4

    Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA

*Department of Chemistry, Swarthmore College, Swarthmore, PA 19081, USA; fax: (610) 328-7355

Publication History

  1. Issue published online: 1 JAN 2009
  2. Article first published online: 1 JAN 2009
  3. Manuscript Accepted: 3 DEC 2004
  4. Manuscript Revised: 30 NOV 2004
  5. Manuscript Received: 10 SEP 2004

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Keywords:

  • transmembrane peptides;
  • helix association;
  • 2H MAS NMR;
  • ATR-FTIR

Abstract

A peptide designed to form a homo-oligomeric transmembrane helical bundle was reconstituted into lipid bilayers and studied by using 2H NMR (nuclear magnetic resonance) with magic angle spinning to confirm that the helical interface corresponds to the interface intended in the design. The peptide belongs to a family of model peptides derived from a membrane-solubilized version of the water-soluble coiled-coil GCN4-P1. The variant studied here contains two asparagines thought to engage in interhelical hydrogen bonding critical to the formation of a stable trimer. For the NMR studies, three different peptides were synthesized, each with one of three consecutive leucines in the transmembrane region deuterium labeled. Prior to NMR data collection, polarized infrared spectroscopy was used to establish that the peptides were reconstituted in lipid bilayers in a transmembrane helical conformation. The 2H NMR line shapes of the three different peptides are consistent with a trimer structure formed by the designed peptide that is stabilized by inter-helical hydrogen bonding of asparagines at positions 7 and 14.

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