All attendees are welcome to participate with poster presentations.  We highly encourage participation from graduate students and post-doctoral scientists.  Six abstracts will be chosen from the submitted abstracts for presentation as short talks.

If you have already registered and need to edit your information, or are ready to upload an abstract, click     HERE. The link for "Abstract Submission" is at the bottom of the page.

If you have not yet registered, click HERE.

Registration will be limited to the first 250 participants, so make plans to register soon!

Abstract Guidelines (download instructions HERE)

Abstract should be uploaded as a Microsoft Word document, be one paragraph in length with a word count of not more than 200. Set right and left margins at 1.25 inch and use 11 point Arial, single spaced, right and left margins justified. Details of style can be seen in the following sample abstract:

6-S-Cysteinylation of bi-covalently attached FAD in berberine bridge enzyme tunes the redox potential for optimal activity

Andreas Winkler,¹ Toni M. Kutchan² and Peter Macheroux¹

¹Graz University of Technology, Institute of Biochemistry, Graz, Austria, ²Donald Danforth Plant Science Center, St. Louis, Missouri, USA

A mutagenic analysis of the amino acid residues His-104 and Cys-166, which are involved in the bi-covalent attachment of FAD to berberine bridge enzyme (BBE), was performed. Here we present a detailed biochemical characterization of the cysteine link to FAD observed in this recently discovered group of flavoproteins. The C166A mutant protein still has residual activity, however, reduced to about 6% of the turnover rate observed for wild-type BBE. A more detailed analysis of single reaction steps by stopped-flow spectrophotometry showed that the reductive half-reaction is greatly influenced by the lack of the 6-S-cysteinyl linkage resulting in a 370-fold decrease in the rate of flavin reduction. Determination of the redox potentials for both wild-type and the C166A mutein revealed that the difference in the redox potential observed can fully account for the change in the kinetic properties. The wild-type protein exhibits a midpoint potential of +132 mV which is the highest redox potential determined for any flavoenzyme so far. Removal of the cysteine linkage to FAD in the C166A mutein leads to a redox potential of +53 mV which is in the expected range for flavoproteins with a single covalent attachment of FAD to a His residue via its 8-alpha position.

Poster Guidelines

Posters should be printed on poster paper with dimensions of not more than 48 x 48 inches. Poster boards will be available at the Danforth Center for mounting your poster.  Space is limited, so please submit your abstract early.

For more information, please contact us.