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.

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Apr 13th, 4:00 PM Apr 13th, 5:00 PM

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.