Bioinformatics and experimental approaches identify families of membrane proteins requiring the co-ordinated action of the Sec pathway and Tat pathways for their integration and define features of the polypeptides that mediate interaction with these pathways.

Coarse-grained modeling reveals a new mechanism for multispanning membrane protein topogenesis, in which misintegrated configurations of the proteins undergo post-translational annealing to reach final, fully integrated multispanning topologies.

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.

ACCuRET is a flexible new method for measuring the structural dynamics of proteins in solution and membrane proteins in their native environment.

There is a strand-based evolutionary mechanism for the diversification of outer membrane proteins, which has implications for how repeat proteins are created and for how outer membrane proteins fold.

Efficient targeting of membrane proteins from the endoplasmic reticulum (ER) to the inner nuclear membrane depends on GTP hydrolysis by Atlastin GTPases and their function in maintaining an interconnected topology of the ER network.

Synthetic single domain antibody libraries and a binder selection cascade encompassing ribosome and phage display enable the selection of conformation-specific binders against previously intractable membrane proteins within three weeks.

A simple, yet elegant method for robust self-assembly of diverse membrane proteins into soluble peptide nanoparticles for their structural and functional analysis in detergent-free solutions.

During cilium-generated signaling, ciliary membrane protein trafficking is unidirectional and ciliary membrane protein composition is regulated through action in the cytoplasm of the retrograde intraflagelllar transport (IFT) motor and shedding of ciliary ectosomes.

A new family of sterol-specific lipid transfer proteins has been found that anchors in the endoplasmic reticulum; some of these proteins stretch across membrane contacts and mediate sterol traffic from the plasma membrane.