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Cation binding induced changes in 15N CSA in a membrane-bound polypeptide

F Tian1, T A Cross

  • 1National High Magnetic Field Laboratory, Florida State University, Tallahassee, Florida, 32306-4005, USA.

Journal of Magnetic Resonance (San Diego, Calif. : 1997)
|January 8, 1999
PubMed
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Cation binding to gramicidin A channels alters spectroscopic signals primarily due to electronic polarizability effects, not structural changes. Solvation by peptide carbonyls induces charge shifts, impacting chemical shifts and dipolar interactions.

Area of Science:

  • Biophysics
  • Structural Biology
  • Spectroscopy

Background:

  • Gramicidin A forms monovalent cation-selective channels.
  • Spectroscopic methods probe molecular structure and dynamics.

Purpose of the Study:

  • To investigate cation binding effects on gramicidin A.
  • To differentiate between structural/dynamic changes and electronic effects.

Main Methods:

  • Solid-state Nuclear Magnetic Resonance (NMR) spectroscopy.
  • Utilized uniformly aligned gramicidin A samples in lipid bilayers.
  • Measured 15N chemical shift tensors and 15N-13C1/15N-2H dipolar interactions.

Main Results:

  • Cation binding induced significant changes in chemical shifts (13C1, 15N) and smaller changes in dipolar interactions.

Related Experiment Videos

  • Observed changes were primarily attributed to through-bond polarizability effects.
  • Partial charges within the peptide backbone were modulated by cation solvation.

    • Conclusions:

    • Cation binding to gramicidin A primarily affects spectroscopic observables via electronic polarizability.
    • Solvation of cations by carbonyl oxygens is key to these electronic effects.
    • Structural or dynamic alterations are not the dominant cause of observed spectroscopic changes.