Event Title
Computational Exploration of Rtt109 Conformers Important for Chromosome Stability
Presentation Type
Poster/Portfolio
Presenter Major(s)
Chemistry, Mathematics
Mentor Information
Mary Karpen, karpenm@gvsu.edu
Department
Chemistry
Location
Kirkhof Center KC24
Start Date
13-4-2011 4:00 PM
End Date
13-4-2011 5:00 PM
Keywords
Life Science, Physical Science
Abstract
Rtt109, a protein that acetylates histones, is required for chromosome stability. Autoacetylation of lysine 290 (K290) is required for Rtt109 function. Crystal structures have shown, however, that the K290 is 11 A (angstroms) from a bound acetyl-coenzyme A, which donates the acetyl group. At this distance, the autoacetylation is impossible. In this study, molecular dynamics simulations are used to determine if conformations of the Rtt109 protein exist in which the autoacetylation is possible.
Computational Exploration of Rtt109 Conformers Important for Chromosome Stability
Kirkhof Center KC24
Rtt109, a protein that acetylates histones, is required for chromosome stability. Autoacetylation of lysine 290 (K290) is required for Rtt109 function. Crystal structures have shown, however, that the K290 is 11 A (angstroms) from a bound acetyl-coenzyme A, which donates the acetyl group. At this distance, the autoacetylation is impossible. In this study, molecular dynamics simulations are used to determine if conformations of the Rtt109 protein exist in which the autoacetylation is possible.