DE-NOVO DESIGN OF INTEGRAL MEMBRANE-PROTEINS

We have designed integral membrane proteins with one, two and four hyd rophobic transmembrane segments of highly simplified amino acid compos ition and with appropriately placed positively charged lysine residues intended to control the overall membrane orientation. When expressed in Escherichia coli, these model proteins insert efficiently into the inner membrane and adopt the predicted topologies. This demonstrates t he feasibility of de novo design of multi-spanning integral membrane p roteins, and opens up new possibilities for membrane protein engineeri ng.