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Related Experiment Videos

Changes in interhelical hydrogen bonding upon rhodopsin activation.

Ashish B Patel1, Evan Crocker, Philip J Reeves

  • 1Departments of Physiology and Biophysics, Center for Structural Biology, Stony Brook University, Stony Brook, NY 11794-5215, USA.

Journal of Molecular Biology
|March 17, 2005
PubMed
Summary

Hydrogen bonds in rhodopsin (visual pigment) shift during activation. This study reveals altered hydrogen bonding in key residues like Trp126, Trp265, and His211, impacting the visual pigment

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Area of Science:

  • Biophysics
  • Structural Biology
  • Spectroscopy

Background:

  • Hydrogen bonding interactions stabilize rhodopsin's inactive state.
  • Previous crystal structures identified key hydrogen bonds involving Glu122, Trp126, Tyr206, His211, Trp265, and Asn302.

Purpose of the Study:

  • To investigate changes in hydrogen bonding during rhodopsin activation using NMR spectroscopy.
  • To elucidate the role of specific hydrogen bonds in the visual pigment activation mechanism.

Main Methods:

  • Solid-state magic angle spinning NMR spectroscopy.
  • Utilized 15N-labeled tryptophan and histidine, and 13C-labeled histidine for detailed analysis.

Main Results:

  • NMR chemical shifts indicated weaker hydrogen bonding for Trp126 and Trp265 indole nitrogens upon activation.

Related Experiment Videos

  • His211 was found to be neutral and became more strongly hydrogen bonded in the activated state (metarhodopsin II).
  • A hydrogen bond between Glu122 and His211 was disrupted in metarhodopsin II.

    • Conclusions:

    • Changes in hydrogen bonding networks are crucial for rhodopsin activation.
    • Specific residue interactions, particularly involving His211 and Glu122, play a significant role in the visual pigment's functional mechanism.