Membrane proteins account for about 20% to 30% of all proteins encoded in a typical
genome. They play central roles in multiple cellular processes mediating the interaction of the
cell with its surrounding. Over 60% of all drug targets contain a membrane domain. The
experimental difficulties of obtaining a crystal structural ...»»»»
Membrane proteins account for about 20% to 30% of all proteins encoded in a typical
genome. They play central roles in multiple cellular processes mediating the interaction of the
cell with its surrounding. Over 60% of all drug targets contain a membrane domain. The
experimental difficulties of obtaining a crystal structural severely limits our ability or
understanding of membrane protein function. Computational evolutionary studies of proteins
are crucial for the prediction of 3D structures. In this project, we construct a tool able to
quantify the evolutionary positive selective pressure on each residue of membrane proteins
through maximum likelihood phylogeny reconstruction. The conservation plot combined with
a structural homology model is also a potent tool to predict those residues that have essentials
roles in the structure and function of a membrane protein and can be very useful in the design
of validation experiments.^^^^