I would be interested in hearing comments on a technique published
recently in Science (262, p.734) to solubilize membrane proteins. This
technique complexes the proteins with an alpha helix with a flat
hydrophobic surface which interacts with the flat hydrophobic surfaces
of the membrane proteins. Results were cited where 85% of
bacteriorhodopsin and 60% of rhodopsin remained in solution in their
native forms after 2 days.
I'm interested in studying the chemistry of membrane proteins. One
constant frustration is that few reliable crystal structures exist for
membrane proteins. Because my background is quantum chemistry rather
than protein crystallography, I'm unfamiliar with the subtleties
involved in crystallizing proteins. How widely applicable is the
technique used in this paper? Can I expect to see hundreds of crystal
structures for membrane proteins flowing into the protein data base,
or am I overestimating the importance of this work? To my eyes the
technique seems to be of monumental impact.
Thanks in advance for any help you can provide.
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Richard P. Muller rpm at wag.caltech.edu
Beckman Institute 139-74 (818) 395-2722 Office
California Institute of Technology (818) 568-9484 Home
Pasadena, California 91124 (818) 568-0918 FAX
