期刊
JOURNAL OF STRUCTURAL BIOLOGY
卷 167, 期 2, 页码 153-158出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jsb.2009.04.011
关键词
High-speed atomic force microscopy; Bacteriorhodopsin; Two-dimensional crystal; Dynamic equilibrium; Trimer; Molecular interaction
资金
- JST CREST
- JSPS Japan
- Bionantechnology IRC
- BBSRC
- Lord Florey
- Grants-in-Aid for Scientific Research [20221006] Funding Source: KAKEN
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.
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