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- Incorporation of photoreceptor membrane into a multilamellar...Incorporation of photoreceptor membrane into a multilamellar film
Biophysical Journal, Volume 31, Issue 1, 1 July 1980, Pages 45-52
K.J. Rothschild, K.M. Rosen and N.A. Clark
AbstractMultilamellar arrays of photoreceptor membrane up to 50 micrometer thick have been produced using a new method. Rhodopsin chromophore orientation in the films was studied using optical linear dichroism. The rhodopsin appears to be structurally intact and capable of photobleaching and regeneration. The production of biologically active liquid-crystal films offers a promising new approach to the study of biomembranes.
Abstract | PDF (1250 kb) - Photoactivation of Rhodopsin Causes an Increased Hydrogen-De...Photoactivation of Rhodopsin Causes an Increased Hydrogen-Deuterium Exchange of Buried Peptide Groups
Biophysical Journal, Volume 74, Issue 1, 1 January 1998, Pages 192-198
Parshuram Rath, Willem J. DeGrip and Kenneth J. Rothschild
AbstractA key step in visual transduction is the light-induced conformational changes of rhodopsin that lead to binding and activation of the G-protein transducin. In order to explore the nature of these conformational changes, time-resolved Fourier transform infrared spectroscopy was used to measure the kinetics of hydrogen/deuterium exchange in rhodopsin upon photoexcitation. The extent of hydrogen/deuterium exchange of backbone peptide groups can be monitored by measuring the integrated intensity of the amide II and amide II′ bands. When rhodopsin films are exposed to DO in the dark for long periods, the amide II band retains at least 60% of its integrated intensity, reflecting a core of backbone peptide groups that are resistant to H/D exchange. Upon photoactivation, rhodopsin in the presence of DO exhibits a new phase of H/D exchange which at 10°C consists of fast (time constant ∼30min) and slow (∼11h) components. These results indicate that photoactivation causes buried portions of the rhodopsin backbone structure to become more accessible.
Abstract | Full Text | PDF (128 kb) - Characterization of Langmuir-Blodgett films of rhodopsin: th...Characterization of Langmuir-Blodgett films of rhodopsin: thermal stability studies
Biophysical Journal, Volume 69, Issue 4, 1 October 1995, Pages 1440-1446
L. Maxia, G. Radicchi, I.M. Pepe and C. Nicolini
AbstractTwo-dimensional close packing of purified bovine rhodopsin, made by the Langmuir-Blodgett technique, was characterized by small angle x-ray scattering and nanogravimetric measurements. The area occupied by a molecule of rhodopsin in the film was approximately 1100 Angstrum2 and the periodicity of the layers resulted in 59 Angstrum. The circular dichroism measurements showed that bleached rhodopsin in Langmuir-Blodgett film had high thermal stability, in fact, reaching a temperature of 150 degrees C without a loss of the secondary structure. Moreover, when the film was made up in the dark, rhodopsin maintained its stability up to at least 200 degrees C and its characteristic absorbance peak at 500 nm up to about 90 degrees C.
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Copyright © 1980 The Biophysical Society. All rights reserved.
Biophysical Journal, Volume 31, Issue 1, 53-64, 1 July 1980
doi:10.1016/S0006-3495(80)85040-5
Articles
A Spectroscopic Study of Rhodopsin Alpha-Helix Orientation
K.J. Rothschild, R. Sanches, T.L. Hsiao and N.A. Clark
Abstract
Polarized Fourier transform infrared spectroscopy and far ultraviolet circular dichroism of oriented multilamellar films of photoreceptor membranes indicate rhodopsin alpha-helices are predominantly oriented perpendicular to the bilayer plane.
