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

被引：64

作者：

Yamashita, Hayato ^{[1
]}

Voitchovsky, Kislon ^{[2
]}

Uchihashi, Takayuki ^{[1
,3
]}

Contera, Sonia Antoranz ^{[2
]}

Ryan, John F. ^{[2
]}

Ando, Toshio ^{[1
,3
]}

机构：

[1] Kanazawa Univ, Dept Phys, Kanazawa, Ishikawa 9201192, Japan

[2] Univ Oxford, Dept Phys, Oxford OX1 3PU, England

[3] JST, CREST, Chiyoda Ku, Tokyo, Japan

来源：

JOURNAL OF STRUCTURAL BIOLOGY | 2009年 / 167卷 / 02期

基金：

英国生物技术与生命科学研究理事会;

关键词：

High-speed atomic force microscopy; Bacteriorhodopsin; Two-dimensional crystal; Dynamic equilibrium; Trimer; Molecular interaction; MEMBRANES; MODEL; VISUALIZATION; DIFFUSION; MOBILITY;

D O I：

10.1016/j.jsb.2009.04.011

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 2009 Elsevier Inc. All rights reserved.

引用

页码：153 / 158

页数：6

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