Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients.

The periplasmic chaperone SurA plays a key role in outer membrane protein (OMP) biogenesis. E. coli SurA comprises a core domain and two peptidylprolyl isomerase domains (P1 and P2), but its mechanisms of client binding and chaperone function have remained unclear.

Mix-Bricks and Flip-Lids: 3D Printed Devices for Simple, Simultaneous Mixing of Reactant Solutions.

Two types of 3D printed devices for simultaneous mixing of small volumes (e.g., 50-500 μL) of reactant solutions are described.

The Dying Art of Vaginal Hysterectomy: A Novel Simulation.

The rate of vaginal hysterectomy has decreased despite the procedure being the preferred hysterectomy method according to the American College of Obstetricians and Gynecologists (ACOG). Physicians have reported that some of the main barriers to performing minimally invasive hysterectomy are the size and shape of the uterus, difficulty of accessibility to the uterus, and surgeons' lack of training and experience. A simulation model for vaginal uterine morcellation was created in an effort to increase surgeons' confidence and to encourage them to select vaginal hysterectomy for their patients.

The Role of SurA PPIase Domains in Preventing Aggregation of the Outer-Membrane Proteins tOmpA and OmpT.

SurA is a conserved ATP-independent periplasmic chaperone involved in the biogenesis of outer-membrane proteins (OMPs). Escherichia coli SurA has a core domain and two peptidylprolyl isomerase (PPIase) domains, the role(s) of which remain unresolved. Here we show that while SurA homologues in early proteobacteria typically contain one or no PPIase domains, the presence of two PPIase domains is common in SurA in later proteobacteria, implying an evolutionary advantage for this domain architecture.

Conformational flexibility within the nascent polypeptide-associated complex enables its interactions with structurally diverse client proteins.

As newly synthesized polypeptides emerge from the ribosome, it is crucial that they fold correctly. To prevent premature aggregation, nascent chains interact with chaperones that facilitate folding or prevent misfolding until protein synthesis is complete. Nascent polypeptide-associated complex (NAC) is a ribosome-associated chaperone that is important for protein homeostasis.