Gezondheid en levenskwaliteit in Brussel

Vaststellingen De jonge Brusselaars verkeren over het algemeen in minder goede gezondheid Het aandeel van de bevolking dat zich in minder goede gezondheid voelt, ligt in het Brussels Gewest boven het Belgische gemiddelde. Dat aandeel bedraagt 29,7% in Wallonië, 27,6% in het Brussels Gewest en 22,2% in Vlaanderen. Indien we rekening houden met de leeftijdsstructuur is de toestand in Wallonië en het Brussels Gewest nog slechter dan de bruto cijfers aangeven. Ondanks de jonge samenstelling van d..

Health and quality of life in Brussels

Observations Overall poorer health of Brussels’ younger generations The proportion of the Brussels-Capital Region’s population that does not consider itself to be in good health is higher than the national mean. The percentages for the various regions are 29.7% in Wallonia, 27.6% in the Brussels Region, and 22.2% in Flanders. If we take account of the population’s age structure, the situations in Wallonia and Brussels are even worse than the raw figures show. Despite the Brussels population’..

Santé et qualité de vie à Bruxelles

Constats Une santé globalement moins bonne pour les jeunes Bruxellois En Région bruxelloise, la proportion de la population qui ne s’estime pas en bonne santé est plus élevée que la moyenne nationale. Cette proportion est de 29,7 % en Wallonie, 27,6 % en Région bruxelloise et 22,2 % en Flandre. Si on tient compte de la structure d’âge, la situation en Wallonie et à Bruxelles est encore plus défavorable que ne le révèlent les chiffres bruts. Malgré la jeunesse de la population bruxelloise, la..

An investigation of Chromatium vinosum high-potential irondashsulfur protein by EPR and Mossbauer spectroscopy; evidence for a freezing-induced dimerization in NaCl solutions

The high-potential irondashsulfur protein (HiPIP) from Chromatium vinosum contains a cubane prosthetic group that shuttles between the [4Fe-4S]3+,2+ states. We find that the EPR spectra from this protein can be explained as a sum of two components, a major one with g=2.02; 2.04; 2.12, and a minor one with g=2.04; 2.07; ~2.13. In the presence of 0.1-2.0 M NaCl, freezing induces polymerization of the protein (presumably dimers), which is detected as intercluster spindashspin interaction in the EPR. The observed spindashspin interactions are interpreted as being due to two very similar dimeric structures in an approx. 1:2 ratio. Computer simulation of the X- and Q-band EPR spectra shows that the z-components of the g-tensors in each dimer pair must be co-linear, with center-to-center distances between the clusters of ~ 13 A and ~ 16 A. Inspection of possible dimeric structures of C. vinosum HiPIP by standard molecular graphics procedures revealed that the Fe/S cluster is exposed toward a flattened surface and is accessible to solvent. Moreover, the Fe/S clusters in two HiPIP molecules can easily achieve a center-to-center distance of ~ 14 A when approaching along a common 3-fold axis that extends through the S4 sulfur atom of the cubane; the z-component of the EPR g-tensor is co-linear with this symmetry axis.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/29129/1/0000168.pd

X-ray Structure of Gelatinase A Catalytic Domain Complexed with a Hydroxamate Inhibitor

Gelatinase A is a key enzyme in the family of matrix metalloproteinases (matrixins) that are involved in the degradation of the extracellular matrix. As this process is an integral part of tumour cell metastasis and angiogenesis, gelatinase is an important target for therapeutic intervention. The X-ray crystal structure of the gelatinase A catalytic domain (GaCD) complexed with batimastat (BB94), a hydroxamate inhibitor, shows an active site with a large S1\u27 specificity pocket. The structure is similar to previously solved structures of stromelysin catalytic domain (SCD) but with differences in VR1 and VR2, two surface-exposed loops on either side of the entrance to the active site. Comparison of GaCD with other members of the matrix metalloproteinase (MMP) family highlights the conservation of key secondary structural elements and the significant differences in the specificity pockets, knowledge of which should enhance our ability to design specific inhibitors for this important anticancer target