| ATP synthase is a membrane protein that uses energy from the transmembrane proton electrochemicai gradient to form ATP from ADP and phosphate [l]Th e enzyme is composed of two major domains, the transmembrane F0 domain and the membrane excluded F1 domain [Z] The current project focuses on the subunit c of the protein, which is an essentiai part of the F0 domain and participates in transmembrane proton conduction. Structural studies indicate that the subunit c arranges into ring structures comprising of 10 -12 subunits in different organisms However, littie is known about the type of interactions that affect the formation of c-rings in the ATPase complex In this project, we further investigate the stability and self aggregation propensity of the c subunit, Molecular dynamics simulations wil1 be performed using a coarse-grain force field [3] t0 define the protein and its membrane environment Simulations wil1 be carried out from a single monomer as weli as the pre-assembied modelled ring structure of the c subunit The stability and dynamics of these systems wil1 be probed and the results wil1 be compared to atomistic simulations [4] Further, simulations wil1 be performed on multiple copies of the monomer to probe the association of these peptides The free energy profile of association of two peptides wil1 be caicuiated. Preliminary results indicate that the subunit has a tendency to assocate in the membrane into dimers and trimers. However, to investigate the more complex decarner interactions, longer time scales and larger length scales need to be investigated |
