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Biophys J, February 2000, p. 683-693, Vol. 78, No. 2

Molecular Dynamics Study of the Nature and Origin of Retinal's Twisted Structure in Bacteriorhodopsin

Emadeddin Tajkhorshid,*dagger Jérôme Baudry,* Klaus Schulten,* and Sándor Suhaidagger

 *Theoretical Biophysics Group, Beckman Institute, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801 USA; and  dagger Department of Molecular Biophysics, German Cancer Research Center, Im Neuenheimer Feld 280, D-69120 Heidelberg, Germany

The planarity of the polyene chain of the retinal chromophore in bacteriorhodopsin is studied using molecular dynamics simulation techniques and applying different force-field parameters and starting crystal structures. The largest deviations from a planar structure are observed for the C13==C14 and C15==N16 double bonds in the retinal Schiff base structure. The other dihedral angles along the polyene chain of the chromophore, although having lower torsional barriers in some cases, do not significantly deviate from the planar structure. The results of the simulations of different mutants of the pigment show that, among the studied amino acids of the binding pocket, the side chain of Trp-86 has the largest impact on the planarity of retinal, and the mutation of this amino acid to alanine leads to chromophore planarity. Deletion of the methyl C20, removal of a water molecule hydrogen-bonded to H15, or mutation of other amino acids to alanine did not show any significant influence on the distortion of the chromophore. The results from the present study suggest the importance of the bulky residue of Trp-86 in the isomerization process, in both ground and excited states of the chromophore, and in fine-tuning of the pKa of the retinal protonated Schiff base in bacteriorhodopsin. The dark adaptation of the pigment and the last step of the bacteriorhodopsin photocycle imply low barriers against the rotation of the double bonds in the Schiff base region. The twisted double bonds found in the present study are consistent with the proposed mechanism of these ground state isomerization events.

Biophys J, February 2000, p. 683-693, Vol. 78, No. 2
© 2000 by the Biophysical Society   0006-3495/00/02/683/11  $2.00


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