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Bridging the Humanitarian-Development Divide : Indonesian-Swedish Stakeholder Case Studies on LRRDEkblad, Peter January 2017 (has links)
This thesis studies the concept of Linking Relief, Rehabilitation and Development (LRRD), a topic discussed since the late 1980’s that has failed to be practically implemented, partly because of widely divergent perspectives on the concept. The discourse on LRRD has so far largely been conducted in a top-down fashion with donors constituting the dominant interlocutor, while the perspectives of aid organisations and local communities involved in humanitarian and developmental programmes have been widely overlooked. This thesis thus means to bring clarity to how LRRD is conceptualised by different stakeholders through proposing a comprehensive conceptual framework based from literature, which is used to analyse empirical case studies at the local, national, and international levels. The case studies were conducted in Indonesia and Sweden through interviews with 16 participants and a survey with 20 beneficiaries as respondents. The participants included: beneficiaries at a tsunami post-disaster site, local community leaders, a local level NGO, two national level Indonesia NGOs (MDMC and YEU), and an INGO (Plan International).The research reveal that none of the cases experienced as rigid divide between humanitarian and development action as is often suggested in the literature discourse and through donor policies. All interviewed NGOs expressed that they operated in a way that does create strong humanitarian-developmental linkages and that the major obstacle to achieve this is external pressures, particularly from donor agencies, to operate under exclusively humanitarian or developmental imperatives.
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The Effect of Salts on the Conformational Stability of ProteinsBeauchamp, David L 13 April 2012 (has links)
It has long been observed that salts affect proteins in a variety of ways, yet comprehensive explanations for different salt effects are still lacking. In the work presented here, the effect of salts on proteins has been investigated through three different effects: the hydrophobic effect; their conformational stability; the hydrogen bonding network of water in a protein’s hydration shell. UV-vis absorbance and fluorescence spectroscopy were used to monitor changes in two model systems, the phenol-acetate contact pair and the model enzyme ribonuclease t1. It was shown that salts affect the hydrophobicity of the contact pair according to their charge density, induced image charges play an important role in the observed salt-induced increase of ribonuclease t1 stability, and that salts affect ribonuclease t1 activity through modulation of the hydrogen bonds of water in the enzyme’s hydration shell. This work contributes a greater understanding of the effect of salts on proteins.
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