On the Folding of Bacteriorhodopsin

  • D. M. Engelman


A great deal of effort has been expended in trying to understand the folding of soluble proteins, the tertiary structures of which have been determined in many cases. The problem has turned out to be very complex, and the current lines of study have met with only limited success. Surprisingly, the possibility of structural prediction may be greater in the case of membrane proteins, where no structures of the membrane spanning regions are yet known at high resolution. This circumstance arises as a consequence of the existence of topological and energetic constraints which place important limits on the range of secondary and tertiary structures expected for globular membrane proteins. In the following discussion, I discuss the energetic arguments as I presently view them, outlining the use of an energy calculation to identify membrane spanning regions from protein sequence information, and considering the covalent, polar, and packing considerations which may be important in the final folding of globular membrane proteins in lipid bilayers.


Lipid Bilayer Purple Membrane Membrane Span Region Nonpolar Environment Nonpolar Region 
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Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • D. M. Engelman
    • 1
  1. 1.Department of Biophysics and BiochemistryYale UniversityNew HavenUSA

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