Caseload midwifery as organisational change:the interplay between professional and organisational projects in Denmark

BACKGROUND: The large obstetric units typical of industrialised countries have come under criticism for fragmented and depersonalised care and heavy bureaucracy. Interest in midwife-led continuity models of care is growing, but knowledge about the accompanying processes of organisational change is scarce. This study focuses on midwives’ role in introducing and developing caseload midwifery. Sociological studies of midwifery and organisational studies of professional groups were used to capture the strong interests of midwives in caseload midwifery and their key role together with management in negotiating organisational change. METHODS: We studied three hospitals in Denmark as arenas for negotiating the introduction and development of caseload midwifery and the processes, interests and resources involved. A qualitative multi-case design was used and the selection of hospitals aimed at maximising variance. Ten individual and 14 group interviews were conducted in spring 2013. Staff were represented by caseload midwives, ward midwives, obstetricians and health visitors, management by chief midwives and their deputies. Participants were recruited to maximise the diversity of experience. The data analysis adopted a thematic approach, using within- and across-case analysis. RESULTS: The analysis revealed a highly interdependent interplay between organisational and professional projects in the change processes involved in the introduction and development of caseload midwifery. This was reflected in three ways: first, in the key role of negotiations in all phases; second, in midwives’ and management’s engagement in both types of projects (as evident from their interests and resources); and third in a high capacity for resolving tensions between the two projects. The ward midwives’ role as a third party in organisational change further complicated the process. CONCLUSIONS: For managers tasked with the introduction and development of caseload midwifery, our study underscores the importance of understanding the complexity of the underlying change processes and of activating midwives’ and managers’ interests and resources in addressing the challenges. Further studies of female-dominated professions such as midwifery should offer good opportunities for detailed analysis of the deep-seated interdependence of professional and organisational projects and for identifying the key dimensions of this interdependence

Temperature dependence of protein dynamics simulated with three different water models

The effect of variation of the water model on the temperature dependence of protein and hydration water dynamics is examined by performing molecular dynamics simulations of myoglobin with the TIP3P, TIP4P, and TIP5P water models and the CHARMM protein force field at temperatures between 20 and 300 K. The atomic mean-square displacements, solvent reorientational relaxation times, pair angular correlations between surface water molecules, and time-averaged structures of the protein are all found to be similar, and the protein dynamical transition is described almost indistinguishably for the three water potentials. The results provide evidence that for some purposes changing the water model in protein simulations without a loss of accuracy may be possible

Structure and Dynamics of Biological Systems: Integration of Neutron Scattering with Computer Simulation

The combination of molecular dynamics simulation and neutron scattering techniques has emerged as a highly synergistic approach to elucidate the atomistic details of the structure, dynamics and functions of biological systems. Simulation models can be tested by calculating neutron scattering structure factors and comparing the results directly with experiments. If the scattering profiles agree the simulations can be used to provide a detailed decomposition and interpretation of the experiments, and if not, the models can be rationally adjusted. Comparison with neutron experiment can be made at the level of the scattering functions or, less directly, of structural and dynamical quantities derived from them. Here, we examine the combination of simulation and experiment in the interpretation of SANS and inelastic scattering experiments on the structure and dynamics of proteins and other biopolymers

Fast Dynamics and Stabilization of Proteins: Binary Glasses of Trehalose and Glycerol

We present elastic and inelastic incoherent neutron scattering data from a series of trehalose glasses diluted with glycerol. A strong correlation with recently published protein stability data in the same series of glasses illustrates that the dynamics at Q ≥ 0.71 Å(−1) and ω > 200 MHz are important to stabilization of horseradish peroxidase and yeast alcohol dehydrogenase in these glasses. To the best of our knowledge, this is the first direct evidence that enzyme stability in a room temperature glass depends upon suppressing these short-length scale, high-frequency dynamics within the glass. We briefly discuss the coupling of protein motions to the local dynamics of the glass. Also, we show that T(g) alone is not a good indicator for the protein stability in this series of glasses; the glass that confers the maximum room-temperature stability does not have the highest T(g)

Anharmonic Behavior in the Multisubunit Protein Apoferritin as Revealed by Quasi-Elastic Neuton Scattering

Quasi-elastic neutron scattering (QENS) has been used to study the deviation from Debye-law harmonic behavior in lyophilized and hydrated apoferritin, a naturally occurring, multisubunit protein. Whereas analysis of the measured mean squared displacement (msd) parameter reveals a hydration-dependent inflection above 240 K, characteristic of diffusive motion, a hydration-independent inflection is observed at 100 K. The mechanism responsible for this low-temperature anharmonic response is further investigated, via analysis of the elastic incoherent neutron scattering intensity, by applying models developed to describe side-group motion in glassy polymers. Our results suggest that the deviation from harmonic behavior is due to the onset of methyl group rotations which exhibit a broad distribution of activated processes (Ea,ave ) 12.2 kJ · mol-1, σ ) 5.0 kJ · mol-1). Our results are likened to those reported for other proteins

From Powder to Solution: Hydration Dependence of Human Hemoglobin Dynamics Correlated to Body Temperature

A transition in hemoglobin (Hb), involving partial unfolding and aggregation, has been shown previously by various biophysical methods. The correlation between the transition temperature and body temperature for Hb from different species, suggested that it might be significant for biological function. To focus on such biologically relevant human Hb dynamics, we studied the protein internal picosecond motions as a response to hydration, by elastic and quasielastic neutron scattering. Rates of fast diffusive motions were found to be significantly enhanced with increasing hydration from fully hydrated powder to concentrated Hb solution. In concentrated protein solution, the data showed that amino acid side chains can explore larger volumes above body temperature than expected from normal temperature dependence. The body temperature transition in protein dynamics was absent in fully hydrated powder, indicating that picosecond protein dynamics responsible for the transition is activated only at a sufficient level of hydration. A collateral result from the study is that fully hydrated protein powder samples do not accurately describe all aspects of protein picosecond dynamics that might be necessary for biological function