Event Title

Insights into the Binding Behavior of Chaperone SurA Using In Silico Methods

Presenter Information

Eric Bell, Oberlin College

Location

Science Center, Bent Corridor

Start Date

10-2-2015 12:00 PM

End Date

10-2-2015 1:20 PM

Poster Number

23

Abstract

The proper folding of many outer membrane proteins of E. coli depends on the chaperone activity of SurA, a protein located in the periplasmic space. The importance of SurA in maintaining the periplasmic proteome suggests small molecules that bind to and inhibit the function of SurA could also disrupt the viability of bacteria. Our lab’s focus is to understand the binding mechanism of not only small molecules but also the client proteins with SurA through a series of computational docking predictions. We used these docking predictions to find good drug candidates using a virtual screen involving the supercomputer, and plan to ultimately test those most promising small molecules in binding studies in vitro. Finally, we hope to further investigate a large-scale conformational change in SurA during binding through creation of disulfide linkages between domains of the protein and observation of its effect on SurA’s chaperone activity.

Major

Biochemistry; Horn Performance

Project Mentor(s)

Lisa Ryno, Chemistry and Biochemistry

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Oct 2nd, 12:00 PM Oct 2nd, 1:20 PM

Insights into the Binding Behavior of Chaperone SurA Using In Silico Methods

Science Center, Bent Corridor

The proper folding of many outer membrane proteins of E. coli depends on the chaperone activity of SurA, a protein located in the periplasmic space. The importance of SurA in maintaining the periplasmic proteome suggests small molecules that bind to and inhibit the function of SurA could also disrupt the viability of bacteria. Our lab’s focus is to understand the binding mechanism of not only small molecules but also the client proteins with SurA through a series of computational docking predictions. We used these docking predictions to find good drug candidates using a virtual screen involving the supercomputer, and plan to ultimately test those most promising small molecules in binding studies in vitro. Finally, we hope to further investigate a large-scale conformational change in SurA during binding through creation of disulfide linkages between domains of the protein and observation of its effect on SurA’s chaperone activity.