Breast feeding practices and views among diabetic women: a retrospective cohort study

Objective: to explore the pattern and experiences of breast-feeding practices among diabetic women. Design: retrospective cohort study using maternal records and postal questionnaires in a Baby-Friendly hospital. Participants: diabetic mothers including women with gestational diabetes, and type 1 and 2 diabetes mellitus. Findings: from the total group of respondents, 81.9% intended to breast feed. The actual breast feeding rates were 81.9% at birth, 68.1% at 2 weeks and 28.7% at 6 months postpartum. Major themes that were identified from women's experiences included information and advice, support vs. pressure, classification and labelling, and expectations. Conclusions: more than two-thirds of the diabetic women intended to breast feed and actually did breast feed in this study. For both the total study population and the type 1 and 2 diabetics alone, more than half were still breast feeding at 2 weeks postpartum, and approximately one-third were still breast feeding at 6 months postpartum. Implications for practice: structured support, provided for women through Baby-Friendly initiatives, was appreciated by the diabetic women in this study. The extent to which this support influenced the highly successful breast feeding practices in this group of women needs focused investigation. The need for a delicate balancing act between pressure and advice in order to prevent coercion was noted.</p

Accelerated X-ray Structure Elucidation of a 36 kDa Muramidase/Transglycosylase Using wARP

The X-ray structure of the 36kDa soluble lytic transglycosylase from Escherichia coli has been determined starting with the multiple isomorphous replacement method with inclusion of anomalous scattering at 2.7 Å resolution. Subsequently, before any model building was carried out, phases were extended to 1.7 Å, resolution with the weighted automated refinement procedure wARP, which gave a dramatic improvement in the phases. The electron-density maps from wARP were of outstanding quality for both the main chain and the side chains of the protein, which allowed the time spent on the tracing, interpretation and building of the X-ray structure to be substantially shortened. The structure of the soluble lyric transglycosylase was refined at 1.7 Å, resolution with X-PLOR to a final crystallographic R factor of 18.9%. Analysis of the wARP procedure revealed that the use of the maximum-likelihood refinement in wARP gave much better phases than least-squares refinement, provided that the ratio of reflections to protein atom parameters was approximately 1.8 or higher. Furthermore, setting aside 5% of the data for an Rfree test set had a negative effect on the phase improvement. The mean WwARP, a weight determined at the end of the wARP procedure and based on the variance of structure factors from six individually refined wARP models, proved to be a better indicator than the Rfree factor to judge different phase improvement protocols. The elongated Slt35 structure has three domains named the alpha, beta and core domains. The alpha domain contains mainly α-helices, while the beta domain consists of a five-stranded antiparallel β-sheet flanked by a short α-helix. Sandwiched between the alpha and beta domains is the core domain, which bears some resemblance to the fold of the catalytic domain of the previously elucidated 70 kDa soluble lytic transglycosylase from E. coli. The putative active site is at the bottom of a large deep groove in the core domain.

Crystal structure of a murine α-class glutathione S-transferase involved in cellular defense against oxidative stress

Glutathione S-transferases (GSTs) are ubiquitous multifunctional enzymes which play a key role in cellular detoxification. The enzymes protect the cells against toxicants by conjugating them to glutathione. Recently, a novel subgroup of α-class GSTs has been identified with altered substrate specificity which is particularly important for cellular defense against oxidative stress. Here, we report the crystal structure of murine GSTA4-4, which is the first structure of a prototypical member of this subgroup. The structure was solved by molecular replacement and refined to 2.9 Å resolution. It resembles the structure of other members of the GST superfamily, but reveals a distinct substrate binding site.

Uncertainties of predictions from parton distribution functions II: the Hessian method

We develop a general method to quantify the uncertainties of parton distribution functions and their physical predictions, with emphasis on incorporating all relevant experimental constraints. The method uses the Hessian formalism to study an effective chi-squared function that quantifies the fit between theory and experiment. Key ingredients are a recently developed iterative procedure to calculate the Hessian matrix in the difficult global analysis environment, and the use of parameters defined as components along appropriately normalized eigenvectors. The result is a set of 2d Eigenvector Basis parton distributions (where d=16 is the number of parton parameters) from which the uncertainty on any physical quantity due to the uncertainty in parton distributions can be calculated. We illustrate the method by applying it to calculate uncertainties of gluon and quark distribution functions, W boson rapidity distributions, and the correlation between W and Z production cross sections.Comment: 30 pages, Latex. Reference added. Normalization of Hessian matrix changed to HEP standar

Kinetic Characterization and X-ray Structure of a Mutant of Haloalkane Dehalogenase with Higher Catalytic Activity and Modified Substrate Range

Conversion of halogenated aliphatics by haloalkane dehalogenase proceeds via the formation of a covalent alkyl-enzyme intermediate which is subsequently hydrolyzed by water. In the wild type enzyme, the slowest step for both 1,2-dichloroethane and 1,2-dibromoethane conversion is a unimolecular enzyme isomerization preceding rapid halide dissociation. Phenylalanine 172 is located in a helix-loop-helix structure that covers the active site cavity of the enzyme, interacts with the Clβ of 1,2-dichloroethane during catalysis, and could be involved in stabilization of this helix-loop-helix region of the cap domain of the enzyme. To obtain more information about the role of this residue in dehalogenase function, we performed a mutational analysis of position 172 and studied the kinetics and X-ray structure of the Phe172Trp enzyme. The Phe172Trp mutant had a 10-fold higher kcat/Km for 1-chlorohexane and a 2-fold higher kcat for 1,2-dibromoethane than the wild-type enzyme. The X-ray structure of the Phe172Trp enzyme showed a local conformational change in the helix-loop-helix region that covers the active site. This could explain the elevated activity for 1-chlorohexane of the Phe172Trp enzyme, since it allows this large substrate to bind more easily in the active site cavity. Pre-steady-state kinetic analysis showed that the increase in kcat found for 1,2-dibromoethane conversion could be attributed to an increase in the rate of an enzyme isomerization step that preceeds halide release. The observed conformational difference between the helix-loop-helix structures of the wild-type enzyme and the faster mutant suggests that the isomerization required for halide release could be a conformational change that takes place in this region of the cap domain of the dehalogenase. It is proposed that Phe172 is involved in stabilization of the helix-loop-helix structure that covers the active site of the enzyme and creates a rigid hydrophobic cavity for small apolar halogenated alkanes.