Structure-function analyses reveal the mechanistic underpinnings of inside-out transmembrane signaling that controls periplasmic proteolysis, and thereby biofilm formation, in bacteria and may be relevant in the context of other signaling proteins with similar control elements.

The chitin-triggered immune response is mediated by a LYK5 and CERK1 receptor complex in Arabidopsis.

The protein CpoB regulates PBP1B activity in response to the Tol energy state, which facilitates feedback and synchronicity between envelope constriction processes during Gram-negative bacterial cell division.

The I_Ks potassium channel complex displays functional flexibility that depends on the ratio of its constituent KCNQ1 and KCNE1 protein subunits.

A fully synthetic library of humanized single domain antibodies yields in vitro high affinity antibodies usable in cell biology and translational projects.

Building on previous work (Pless, 2013), we argue that side-chain 'flip out' is a key event in potassium channel C-type inactivation, and propose a new method for encoding multiple noncanonical amino acids and controlling protein stoichiometry.

Cyanine fluorophores are encoded as non-canonical amino acids to produce functional proteins in cell-free translation systems and live cells for single-molecule imaging.

Biochemical dissections show that the Guided Entry of Tail Anchored proteins (GET) pathway selects ER-destined tail-anchored proteins using at least two distinct molecular mechanisms, each recognizing a distinct physicochemical feature in the substrate.

First two transmembrane segments of Tim17 are involved in interaction with the channel and the second two with the motor of the presequence translocase suggesting how proteins are handed over during their translocation into mitochondria.

The motor that drives preproteins into the mitochondrial matrix is coupled to the translocase by Tim44, a two-domain scaffold protein with an intrinsically disordered "dynamic arm" and a structurally stable anchoring domain.