15 research outputs found
Pro poor accountability in Watsan at Ahmedabad, India
Traditionally, provision of water and sanitation at the household level to slum residents was not seen as a priority by ULBs:
the mechanisms for obtaining such services were typically absent. The vacuum was filled by middlemen, who charged
huge amounts for sub-standard services. In Ahmedabad City, India, the ULB, slum residents and NGOs have developed
an innovative system to bring accountability and reduced corruption to the provision of watsan services. The mainstay of
the system is charging affordable user fees, this ensures that the users – slum residents – have leverage to ensure quality
in the installation and maintenance of services. The paper starts by describing the traditional approach to the provision
of water and sanitation before presenting the innovation. Pro-poor accountability arrangements are then listed. Three
examples follow that show what happened when the innovation was put into practice; the first is of a slum, the second of
a middleman and the third of a resident
Side chain SASA behavior for Cysteine 176 (A), Histidine (B), Cysteine 238 (C) and Cysteine 242 (D) at 300 K and 310 for R175H.
<p>Side chain SASA behavior for Cysteine 176 (A), Histidine (B), Cysteine 238 (C) and Cysteine 242 (D) at 300 K and 310 for R175H.</p
Comparison of <sup><i>opt</i></sup>ΔΔ<i>G<sub>bind</sub></i> for the p53 <i>ts</i>-mutants against wild type at both 300 K and 310 K.
<p>Comparison of <sup><i>opt</i></sup>ΔΔ<i>G<sub>bind</sub></i> for the p53 <i>ts</i>-mutants against wild type at both 300 K and 310 K.</p
Side chain SASA behavior for Valine in WT and Alanine in V143A at 143rd position at 300 K (A) and 310 K (B).
<p>Side chain SASA behavior for Valine in WT and Alanine in V143A at 143rd position at 300 K (A) and 310 K (B).</p
Average values for free energy in binding of the eight interface residues for WT, V143A, R249S and R175H at 300 K (A) and 310 K (B) (error bars indicate standard deviation).
<p>Average values for free energy in binding of the eight interface residues for WT, V143A, R249S and R175H at 300 K (A) and 310 K (B) (error bars indicate standard deviation).</p
Average values for side chain SASA of the eight interface residues for WT, V143A, R249S and R175H at 300 K (A) and 310 K (B) (error bars indicate standard deviation).
<p>Average values for side chain SASA of the eight interface residues for WT, V143A, R249S and R175H at 300 K (A) and 310 K (B) (error bars indicate standard deviation).</p
Population distribution based on Relative SASA and Relative Δ G<sub><i>protein</i></sub>, % population less stable than WT at 300 K has been given in red color.
<p>Population distribution based on Relative SASA and Relative Δ G<sub><i>protein</i></sub>, % population less stable than WT at 300 K has been given in red color.</p
Free energy of p53 molecule throughout the 30 ns for WT at 300 K (black), V143A (red), R249S (green) and R175H (blue) at 310 K.
<p>Free energy of p53 molecule throughout the 30 ns for WT at 300 K (black), V143A (red), R249S (green) and R175H (blue) at 310 K.</p
Synthesis and in Vitro Evaluation of a Biotinylated Dextran-Derived Probe for Molecular Imaging
Herein we report the design, synthesis, and in vitro evaluation
of a gadolinium-containing biotinylated dextran-derived moleÂcular
imaging probe as a prospective neuroanatomical tracer by means of
magnetic resonance imaging (MRI). The probe was effectively taken
up by cultured differentiated murine neuroblastoma cells and significantly
enhanced the contrast in <i>T</i><sub>1</sub>- and <i>T</i><sub>2</sub>-weighted MR images of labeled cells under
physiological conditions. A significant longitudinal relaxation rate
enhancement in the presence of avidin was observed allowing the verification
of the results in the end of noninvasive longitudinal MRI connectivity
studies by post-mortem histology. The in vitro results indicate that
the probe has the potential to be used in vivo to identify the organization
of global neuronal networks in the brain with MRI
Free energy distribution of p53 molecule along principal component 2 calculated using <i>ψ</i> dihedrals at 300 K and 310 K.
<p>Free energy distribution of p53 molecule along principal component 2 calculated using <i>ψ</i> dihedrals at 300 K and 310 K.</p