Contributed Lecture
The Membrane Proteome Dynamic Fold Space

The membrane proteome constitutes over a quarter of the proteome and the majority of drug targets yet constitutes less than 2% of the protein databank and is far less understood compared to its soluble counterpart. We have recently shown that the membrane- and soluble-protein helix-helix interactome are geometrically identical yet are governed by different interactions (Structure 2015 23:527-41). Small residues and backbone-mediated hydrogen bonds govern membrane proteome dynamic folding while the hydrophobic effect does so for the soluble proteome. To understand these features we developed novel analysis of crystal structure flexibility and geometric profiles (http://helixgeometry.weizmann.ac.il and http://bfactor.weizmann.ac.il). I will describe how such an analysis along with biochemical and biophysical characterization elucidates the protein-gated mechanism of photosynthesis. More generally, the analysis of a membrane proteome non-redundant dataset presents general guidelines explaining the apparently contradicting requirements of membrane proteins for stability, hydrophobicity and dynamic functionality.