Sankararamakrishnan, R and Vishveshwara, S (1992) The structures of bacteriorhodopsin with different retinal-Schiff base orientations--computer modeling and energy minimization studies. In: Journal of Biomolecular Structure & Dynamics, 9 (6). pp. 1073-1095.Full text not available from this repository.
Bacteriorhodopsin has been the subject of intense study in order to understand its photochemical function. The recent atomic model proposed by Henderson and coworkers based on electron cryo-microscopic studies has helped in understanding many of the structural and functional aspects of bacteriorhodopsin. However, the accuracy of the positions of the side chains is not very high since the model is based on low-resolution data. In this study, we have minimized the energy of this structure of bacteriorhodopsin and analyzed various types of interactions such as - intrahelical and interhelical hydrogen bonds and retinal environment. In order to understand the photochemical action, it is necessary to obtain information on the structures adopted at the intermediate states. In this direction, we have generated some intermediate structures taking into account certain experimental data, by computer modeling studies. Various isomers of retinal with 13-cis and/or 15-cis conformations and all possible staggered orientations of Lys-216 side chain were generated. The resultant structures were examined for the distance between Lys-216-schiff base nitrogen and the carboxylate oxygen atoms of Asp-96 - a residue which is known to reprotonate the schiff base at later stages of photocycle. Some of the structures were selected on the basis of suitable retinal orientation and the stability of these structures were tested by energy minimization studies. Further, the minimized structures are analyzed for the hydrogen bond interactions and retinal environment and the results are compared with those of the minimized rest state structure. The importance of functional groups in stabilizing the structure of bacteriorhodopsin and in participating dynamically during the photocycle have been discussed.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Adenine Press.|
|Keywords:||Vibrational Spectroscopy;Proton Translocation;Chromophore Isomerization;Photochemical Cycle;Purple Membrane;Amino-Acids;Light;Substitution;Proteins;Mutants.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||30 May 2011 05:19|
|Last Modified:||30 May 2011 05:19|
Actions (login required)