Menstrual management: a neglected aspect of hygiene interventions

Purpose - Effective menstrual management is essential for the mental and physical well being of women. However, many women in low-income countries lack access to the materials and facilities required. They are thus restricted in their activities whilst menstruating thus compromising their education, income and domestic responsibilities. The paper aims to discuss these issues. Design/methodology/approach - This study describes the menstrual management challenges faced by women in an emergency situation in Uganda. Totally, 50 interviews and focus group discussions were conducted with women from villages, internally displaced person (IDP) camps and schools so that the menstrual management of the host population could be compared with the IDPs. Findings - This study showed that in IDP camps there was a significant lack of materials including soap, underpants and absorbing cloth, and facilities like latrines and bathing shelters. As a consequence women in IDP camps suffer with poor health and diminished dignity. There is also a lack of education about menstruation and reproductive health and practices are strongly influenced by cultural taboos. Originality/value - This is the first time that the menstrual management of women in IDP or refugee camps has been studied

The interaction of the Ada protein with DNA : structure and thermodynamics

The C-terminal domain of the E. coli Ada protein (Ada-C) aids the maintenance of genomic integrity by efficiently repairing pre-mutagenic O6-alkylguanine lesions in DNA. The aim of this thesis was to discern the manner in which Ada-C binds and repairs DNA. The research was pursued from both structural and thermodynamic perspectives, to obtain a model of the DNA-binding process.;The production of recombinant Ada-C from E. coli culture was enhanced through a combination of rational media design, E. coli strain choice, and the employment of a growth strategy for maximising cell density prior to induction of protein expression.;Nuclear Magnetic Resonance (NMR) studies mapped the DNA-binding site to the recognition helix of the helix-turn-helix motif and a loop region (residues 149-155) known as the 'wing'. Using this binding interface, and in the absence of a large conformational change in the protein upon DNA-binding, it was found that an O6 meG lesion was inaccessible to active site nucleophile Cys 144 when the lesion remained stacked within the DNA duplex. This lesion could enter the active site by being rendered extrahelical, or "flipping".;The DNA-binding process was shown to be entropically driven, whilst the demethylation reaction provoked an exothermic heat change. At millimolar concentrations, methylation of Ada-C led to a loss of structural integrity.;Duplex DNA containing an O6meG lesion had a lower enthalpy of melting than unmethylated DNA. This, along with 19F NMR work on modified DNA, led to the postulation that O6meG might induce localised duplex melting. This would certainly aid the base-flipping process

DNA-binding mechanism of the Escherichia coli Ada O(6)-alkylguanine–DNA alkyltransferase

The C-terminal domain of the Escherichia coli Ada protein (Ada-C) aids in the maintenance of genomic integrity by efficiently repairing pre-mutagenic O(6)-alkylguanine lesions in DNA. Structural and thermodynamic studies were carried out to obtain a model of the DNA-binding process. Nuclear magnetic resonance (NMR) studies map the DNA-binding site to helix 5, and a loop region (residues 151–160) which form the recognition helix and the ‘wing’ of a helix–turn–wing motif, respectively. The NMR data also suggest the absence of a large conformational change in the protein upon binding to DNA. Hence, an O(6)-methylguanine (O(6)meG) lesion would be inaccessible to active site nucleophile Cys146 if the modified base remained stacked within the DNA duplex. The experimentally determined DNA-binding face of Ada-C was used in combination with homology modelling, based on the catabolite activator protein, and the accepted base-flipping mechanism, to construct a model of how Ada-C binds to DNA in a productive manner. To complement the structural studies, thermodynamic data were obtained which demonstrate that binding to unmethylated DNA was entropically driven, whilst the demethylation reaction provoked an exothermic heat change. Methylation of Cys146 leads to a loss of structural integrity of the DNA-binding subdomain

DNA-binding mechanism of the <i>Escherichia coli</i> Ada O⁶-alkylguanine-DNA alkyltransferase

The C-terminal domain of the Escherichia coli Ada protein (Ada-C) aids in the maintenance of genomic integrity by efficiently repairing pre-mutagenic O:(6)-alkylguanine lesions in DNA. Structural and thermodynamic studies were carried out to obtain a model of the DNA-binding process. Nuclear magnetic resonance (NMR) studies map the DNA-binding site to helix 5, and a loop region (residues 151-160) which form the recognition helix and the 'wing' of a helix-turn-wing motif, respectively. The NMR data also suggest the absence of a large conformational change in the protein upon binding to DNA. Hence, an O:(6)-methylguanine (O:(6)meG) lesion would be inaccessible to active site nucleophile Cys146 if the modified base remained stacked within the DNA duplex. The experimentally determined DNA-binding face of Ada-C was used in combination with homology modelling, based on the catabolite activator protein, and the accepted base-flipping mechanism, to construct a model of how Ada-C binds to DNA in a productive manner. To complement the structural studies, thermodynamic data were obtained which demonstrate that binding to unmethylated DNA was entropically driven, whilst the demethylation reaction provoked an exothermic heat change. Methylation of Cys146 leads to a loss of structural integrity of the DNA-binding subdomain