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

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 indi...

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Publication status:
Published

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Publisher copy:
10.1016/j.jsb.2009.04.011

Authors


Yamashita, H More by this author
Voïtchovsky, K More by this author
Uchihashi, T More by this author
Contera, SA More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Physics, Condensed Matter Physics
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Journal:
Journal of structural biology
Volume:
167
Issue:
2
Pages:
153-158
Publication date:
2009-08-05
DOI:
EISSN:
1095-8657
ISSN:
1047-8477
URN:
uuid:915f3de0-fb46-4406-9777-ff4a036e7b85
Source identifiers:
21122
Local pid:
pubs:21122

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