Allied health pre-entry student clinical placement capacity: can it be sustained?

Objective Meeting the demand for clinical placements in an environment of increasing university cohort growth and changes in health service delivery models is challenging. This paper describes the outcomes of a quality review activity designed to gain key stakeholder perspectives on the enablers and barriers to sustaining effort to placement provision and reports on: (1) measures used to determine the effect of a jurisdiction-wide initiative in clinical education for five allied health professions; (2) outcomes of data related to key factors affecting placement supply and demand; and (3) qualitative perspectives from management, workforce and university stakeholders on placement sustainability. Methods This study reviewed clinical placement, staff full-time equivalent numbers, university program and student cohort data for five allied health professions from 2013 to 2016.

Growth Restriction in Infants and Young Children with Congenital Heart Disease.

Objective: The purpose of this study was to determine the prevalence of growth restriction in infants and young children with congenital heart disease (CHD) and investigate the relationship between poor growth, feeding difficulties, cardiac classification, and nutrition intervention on outcomes.

Design: This is a prospective observational cohort study of infants and young children with CHD aged 0-3 years admitted to hospital for cardiac surgery. Anthropometry, growth history, cardiac classification, cardiac diagnosis, feeding difficulty, and nutrition intervention data were collected for 78 participants.

Mutagenesis of morphinone reductase induces multiple reactive configurations and identifies potential ambiguity in kinetic analysis of enzyme tunneling mechanisms.

We have identified multiple reactive configurations (MRCs) of an enzyme-coenzyme complex that have measurably different kinetic properties. In the complex formed between morphinone reductase (MR) and the NADH analogue 1,4,5,6-tetrahydro-NADH (NADH4) the nicotinamide moiety is restrained close to the FMN isoalloxazine ring by hydrogen bonds from Asn-189 and His-186 as determined from the X-ray crystal structure. Molecular dynamic simulations indicate that removal of one of these hydrogen bonds in the N189A MR mutant allows the nicotinamide moiety to occupy a region of configurational space not accessible in wild-type enzyme.