Presenter(s): Anson Dang
Faculty Mentor(s): Andrew Marcus & Peter von Hippel
Poster 67
Session: Sciences
The single-stranded (ss)DNA binding protein (gp32) of bacteriophage T4 plays a central role in regulating the functions and integration of the helicase, polymerase and primase components of the T4 DNA replication system. The T4 replication system serves as an excellent model for higher organisms as it contains all the essential components for DNA replication. This project aims to investigate how polarity and length of the ssDNA affect gp32 DNA binding. We perform microseconds resolution single-molecule FRET (smFRET) measurements on four primer templates of 14-15 base pairs and different polarities. Data are analyzed using both second- and fourth- order time correlation functions. At the current stage of this project, our results indicate at least three different conformational stages for gp32 binding. Further analysis is required to compare if and how gp32 dimer bind differently on the different constructs.