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

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Abstract

金沢大学理工研究域 数物科学系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 -0.9 kcal/mol. Rotational motion of individual bound trimers indicates that the inter-trimer bond involves W10-W12 tryptophan residues. © 2009 Elsevier Inc. All rights reserved.最終稿を登録可能.

Journal

  • Journal of structural biology

    Journal of structural biology 167(2), 153-158, 2009-08-01

    Elsevier / Academic Press

Cited by:  3

Codes

  • NII Article ID (NAID)
    120001491369
  • NII NACSIS-CAT ID (NCID)
    AA10761632
  • Text Lang
    ENG
  • Article Type
    Journal Article
  • ISSN
    1047-8477
  • Data Source
    CJPref  IR 
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