Abstract
Membrane protein tertiary or quaternary structure study is important for understanding molecular mechanism. X-ray crystallography is one commonly used method for resolving membrane protein structure, however it is easy for proteins to denature or aggregate in the purification process when proteins are solubilized in detergent in this method. With combining experimental residues distance results such as FRET (Fluorescence resonance energy transfer) data, computation 3D structural prediction provides a new way to predict membrane protein tertiary or quaternary structure. Taking CtH+-PPase as a research object in this study, we try to combine homology modeling, empirical potential and FRET data to predict membrane protein quaternary structure. The final molecular dynamics simulation refined structure reveals that CtH+-PPase is a intercrossing membrane protein with 29.8 degree angle between two monomers and RMSD between CtH+-PPase SWISSMODEL and MD result is 22.6 Å.