Folding and insertion of melittin in membrane mimics

AEI 27

Matthew R. Hartings, hartings@caltech.edu1, Harry B. Gray1, and Jay R. Winkler2. (1) Beckman Institute, California Institute of Technology, Pasadena, CA 91125, (2) Beckman Institute, California Insitute of Technology, Pasadena, CA 91125
The peptide toxin mellitin, the primary component of bee venom, forms stable structures in both aqueous and membrane environments. We have investigated the energetics of structure formation and membrane insertion for the wild-type peptide, which is a random coil in aqueous solution, as well as for several mutants. We have found that single point mutations in the primary sequence induce helical structure in the peptide, even in aqueous environments. Analysis of fluorescence energy transfer from a tryptophan donor to a nitrotyrosine acceptor in a selectively labeled mutant indicates that the peptide adopts a bent helical structure when inserted into lipid vesicles.
 

Academic Employment Initiative
8:00 PM-10:00 PM, Monday, August 20, 2007 BCEC -- Exhibit Hall - B2, Sci-Mix

Academic Employment Initiative

The 234th ACS National Meeting, Boston, MA, August 19-23, 2007