Inhibition of C. elegans FLD-1 or Human TLCD1/2 prevents saturated fat lipotoxicity by allowing increased levels of membrane phospholipids that contain fluidizing long-chain polyunsaturated fatty acids.
Key sequence motifs, defined using the first reported structure of a monotopic membrane protein with a reentrant helix, enable identification of new monotopic membrane protein families previously predicted as membrane spanning.
An unexpected new biological function was discovered for the universally conserved cofactor lipoate, as lipoate-binding proteins proved essential for a novel wide-spread prokaryotic sulfur oxidation pathway.
A new method of protein structure prediction that incorporates residue–residue co-evolution information into the Rosetta structure prediction program was used to develop models for 58 large protein families that had no previous structural information.
Structure, dynamics, and mutation of a gamete fusion protein and comparisons to viral homologues suggest that after trimerization the domain bearing the membrane-inserting fusion loops can pivot with respect to the trimer 3-fold axis.