New ways for our families : Designing an Aboriginal and Torres Strait Islander cultural practice framework and system responses to address the impacts of domestic and family violence on children and young people

Little has been done to understand what works to support First Nations children and young people to heal from their experiences of violence. This research project explores how services and systems can better respond to the needs of Aboriginal and Torres Strait Islander children and young people exposed to DFV who come to the attention of child protection systems. Led by the Queensland Aboriginal and Torres Strait Islander Child Protection Peak (QATSICPP), a team of First Nations researchers, supported by non-Indigenous researchers, utilised a participatory action research methodology – ensuring cultural safety and adherence to cultural values and protocols, including co-creation of knowledge. This report, the first in a series for this project, presents the results of a literature review and the findings from the initial cycles of action research conducted with Aboriginal and Torres Strait Islander chief investigators, community researchers and practitioners working in eight community-controlled child and family services across Queensland. The literature review and the outcomes of the initial action research cycle confirmed that the experience of DFV in childhood is resulting in negative lifelong outcomes for First Nations children, including increased interactions with the child protection and justice systems. The researchers also found that these responses (child protection and justice) are not adequate or culturally safe. To support healing for these children and young people, the report recommends: • holistic healing opportunities • culturally strong and community-led whole-of-family support • therapeutic healing circles and camps • connection to and knowledge about traditional cultural values, systems and traditions • a framework of perpetrator accountability • system changes include procuring place-based and healing responses for Aboriginal and Torres Strait Islander community-controlled services that support self-determination, and working collectively with the whole family. Additionally, cultural capability across the service system needs to be enhanced, and structural racism needs to be eliminated in order to reduce the load on existing Aboriginal and Torres Strait Islander services. Future publications from this research project, due in 2022, will consist of a research report on the remaining action research cycles and a framework for working with Aboriginal and Torres Strait Islander children and young people who have experienced DFV and have also come in contact with the child protection system

Protein Stabilization and the Hofmeister Effect: The Role of Hydrophobic Solvation

Using the IGg binding domain of protein L from Streptoccocal magnus (ProtL) as a case study, we investigated how the anions of the Hofmeister series affect protein stability. To that end, a suite of lysine-to-glutamine modifications were obtained and structurally and thermodynamically characterized. The changes in stability introduced with the mutation are related to the solvent-accessible area of the side chain, specifically to the solvation of the nonpolar moiety of the residue. The thermostability for the set of ProtL mutants was determined in the presence of varying concentrations (0–1 M) of six sodium salts from the Hofmeister series: sulfate, phosphate, fluoride, nitrate, perchlorate, and thiocyanate. For kosmotropic anions (sulfate, phosphate, and fluoride), the stability changes induced by the cosolute (encoded in m3=δΔG0/δC3) are proportional to the surface changes introduced with the mutation. In contrast, the m3 values measured for chaotropic anions are much more independent of such surface modifications. Our results are consistent with a model in which the increase in the solution surface tension induced by the anion stabilizes the folded conformation of the protein. This contribution complements the nonspecific and weak interactions between the ions and the protein backbone that shift the equilibrium toward the unfolded state