Efficient whole-brain tract-specific T mapping at 3T with slice-shuffled inversion-recovery diffusion-weighted imaging.

Purpose: Most voxels in white matter contain multiple fiber populations with different orientations and levels of myelination. Conventional T mapping measures 1 T value per voxel, representing a weighted average of the multiple tract T times. Inversion-recovery diffusion-weighted imaging (IR-DWI) allows the T times of multiple tracts in a voxel to be disentangled, but the scan time is prohibitively long.

Collaborative Active Learning Activities Promote Deep Learning in a Chemistry-Biochemistry Course.

Currently in higher education, there is a move towards providing more student-centred learning experiences, where students are actively involved in the learning process. To promote learner engagement and communication between peers, many educators utilise collaborative active learning activities. This study aimed to demonstrate that an active learning curriculum developed for a Chemistry-Biochemistry unit, allowed students to gain a deep understanding of the content, while developing key academic skills.

Structural analysis of variant of Helicobacter pylori MotB in its activated form, engineered as chimera of MotB and leucine zipper.

Rotation of the bacterial flagellum is powered by a proton influx through the peptidoglycan (PG)-tethered stator ring MotA/B. MotA and MotB form an inner-membrane complex that does not conduct protons and does not bind to PG until it is inserted into the flagellar motor. The opening of the proton channel involves association of the plug helices in the periplasmic region of the MotB dimer into a parallel coiled coil.

Design, purification and characterization of a soluble variant of the integral membrane protein MotB for structural studies.

The bacterial flagellar motor is an intricate nanomachine powered by a transmembrane electrochemical gradient. Rotation is driven by the cumulative action of several peptidoglycan-anchored stator complexes on the rotor. In proton-motive force-driven motors, the stator complex is composed of a motility protein B (MotB) dimer surrounded by four copies of MotA, where both MotA and MotB are integral membrane proteins.

Crystallographic and molecular dynamics analysis of loop motions unmasking the peptidoglycan-binding site in stator protein MotB of flagellar motor.

Background: The C-terminal domain of MotB (MotB-C) shows high sequence similarity to outer membrane protein A and related peptidoglycan (PG)-binding proteins. It is believed to anchor the power-generating MotA/MotB stator unit of the bacterial flagellar motor to the peptidoglycan layer of the cell wall. We previously reported the first crystal structure of this domain and made a puzzling observation that all conserved residues that are thought to be essential for PG recognition are buried and inaccessible in the crystal structure.