application) This revised application aims to apply Dr. Caffrey's expertise in lipids to the rational design of cubic lipid phases for the crystallization of membrane proteins. Though a number of membrane proteins, notably bacteriorhodopsin (BR), have been successfully crystallized from lipid cubic mesophases, there has been no careful study of the optimum state of the mesophase, and of the details of the boundary between the growing crystal and the bulk phase. Instead only empirical procedures are used to obtain crystals. To remedy this, Dr. Caffrey proposes to extend his library of phase diagrams for monoacylglycerols, which form cubic mesophases, and to study the relationship between the phase diagrams and the optimum crystallization of BR and of a bacterial photoreaction center, RC. The results of these studies, together with an analysis in detail of the crystal/lipid interface will then be used in attempts at rational crystallization of the previously uncrystallized photosystem II from Chlamydomonas.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
1R01GM061070-01A1
Application #
6285859
Study Section
Biophysical Chemistry Study Section (BBCB)
Program Officer
Chin, Jean
Project Start
2001-01-01
Project End
2004-12-31
Budget Start
2001-01-01
Budget End
2001-12-31
Support Year
1
Fiscal Year
2001
Total Cost
$242,856
Indirect Cost
Name
Ohio State University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
098987217
City
Columbus
State
OH
Country
United States
Zip Code
43210
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Siegel, D P; Cherezov, V; Greathouse, D V et al. (2006) Transmembrane peptides stabilize inverted cubic phases in a biphasic length-dependent manner: implications for protein-induced membrane fusion. Biophys J 90:200-11

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