Display Settings:

Format

Send to:

Choose Destination
J Struct Biol. 2009 Aug;167(2):153-8. doi: 10.1016/j.jsb.2009.04.011. Epub 2009 May 3.

Dynamics of bacteriorhodopsin 2D crystal observed by high-speed atomic force microscopy.

Author information

  • 1Department of Physics, Kanazawa University, Kakuma-machi, Kanazawa, Japan. yhayato@stu.kanazawa-u.ac.jp

Abstract

We have used high-speed atomic force microscopy to study the dynamics of bacteriorhodopsin (bR) molecules at the free interface of the crystalline phase that occurs naturally in purple membrane. Our results reveal temporal fluctuations at the crystal edges arising from the association and dissociation of bR molecules, most predominantly pre-formed trimers. Analysis of the dissociation kinetics yields an estimate of the inter-trimer single-bond energy of -0.9kcal/mol. Rotational motion of individual bound trimers indicates that the inter-trimer bond involves W10-W12 tryptophan residues.

PMID:
19416755
[PubMed - indexed for MEDLINE]

LinkOut - more resources

Full Text Sources

Other Literature Sources

Molecular Biology Databases

PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Icon for Elsevier Science
    Loading ...
    Write to the Help Desk