Structural changes in bacteriorhodopsin in response to alternate illumination observed by high-speed atomic force microscopy.
نویسندگان
چکیده
منابع مشابه
High-speed atomic force microscopy shows dynamic molecular processes in photoactivated bacteriorhodopsin.
Dynamic changes in protein conformation in response to external stimuli are important in biological processes, but it has proved difficult to directly visualize such structural changes under physiological conditions. Here, we show that high-speed atomic force microscopy can be used to visualize dynamic changes in stimulated proteins. High-resolution movies of a light-driven proton pump, bacteri...
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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 ...
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In this paper, the non-linear dynamic response of rectangular atomic force microscopy in tapping mode is considered. The effect of cantilever’s geometrical parameters (e.g., cantilever length, width, thickness, tip length and the angle between the cantilever and the sample's surface in liquid environment has been studied by taking into account the interaction forces. Results indicate that the r...
متن کاملRole of trimer-trimer interaction of bacteriorhodopsin studied by optical spectroscopy and high-speed atomic force microscopy.
Bacteriorhodopsin (bR) trimers form a two-dimensional hexagonal lattice in the purple membrane of Halobacterium salinarum. However, the physiological significance of forming the lattice has long been elusive. Here, we study this issue by comparing properties of assembled and non-assembled bR trimers using directed mutagenesis, high-speed atomic force microscopy (HS-AFM), optical spectroscopy, a...
متن کاملStructural changes of purple membrane and bacteriorhodopsin during its denaturation induced by high pH.
Bacteriorhodopsin (bR) trimers naturally form two-dimensional hexagonal crystals in purple membrane (PM), which make it very stable. However, the dnaturation of bR was found to occur during a very narrow pH range when the pH was increased above 12.0, as indicated by inactivation of the photochemical cycle observed by flash photolysis kinetic spectra. Here, atomic force microscopy was used to st...
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ورودعنوان ژورنال:
- Angewandte Chemie
دوره 50 19 شماره
صفحات -
تاریخ انتشار 2011