Levels and predictors of happiness in the south of the islamic republic of iran Niveau et facteurs prédictifs de bonheur dans le sud de la république islamique d�iran

Background: Happiness is considered an index of the development of human society and well-being in the world. Aims: The aim of this study was to measure the level of happiness in a middle sized Iranian city (Kerman) using 2 instru-ments and the predictor factors. Methods: In a cross-sectional study, 1000 adults were questioned using multi-stage cluster sampling in 2016. The LoH was assessed using the Oxford Happiness Inventory (OHI) and a self-report questionnaire. The level of physical activity and the religion index were assessed using standard questionnaires. Results: The results of 2 questionnaires had a statistically significant correlation with measuring level of happiness (Pearson correlation coefficient 0.69; P-value < 0.001). Around 90 of participants stated that they had moderate to high LoH, but the mean happiness score based on the OHI was 43.2 (43.7 in men, 42.7 in women). Illiteracy, unemployment, divorce, living in deprived areas, high level of stress, weak religious beliefs and practice, lower income, and poor health significantly decreased the LoH score. Conclusion: Level of happiness is relatively low in Kerman. There are effective evidence-based interventions that might promote the LoH of the population, including promoting the level of community health, educating for stress management and improving access to urban facilities in deprived areas. © World Health Organization (WHO) 2020

Native disulphide-linked dimers facilitate amyloid fibril formation by bovine milk alpha(S2)-casein

Bovine milk α(S2)-casein, an intrinsically disordered protein, readily forms amyloid fibrils in vitro and is implicated in the formation of amyloid fibril deposits in mammary tissue. Its two cysteine residues participate in the formation of either intra- or intermolecular disulphide bonds, generating monomer and dimer species. X-ray solution scattering measurements indicated that both forms of the protein adopt large, spherical oligomers at 20 °C. Upon incubation at 37 °C, the disulphide-linked dimer showed a significantly greater propensity to form amyloid fibrils than its monomeric counterpart. Thioflavin T fluorescence, circular dichroism and infrared spectra were consistent with one or both of the dimer isomers (in a parallel or antiparallel arrangement) being predisposed toward an ordered, amyloid-like structure. Limited proteolysis experiments indicated that the region from Ala⁸¹ to Lys¹¹³ is incorporated into the fibril core, implying that this region, which is predicted by several algorithms to be amyloidogenic, initiates fibril formation of α(S2)-casein. The partial conservation of the cysteine motif and the frequent occurrence of disulphide-linked dimers in mammalian milks despite the associated risk of mammary amyloidosis, suggest that the dimeric conformation of α(S2)-casein is a functional, yet amyloidogenic, structure.David C. Thorn, Elmira Bahraminejad, Aidan B. Grosas, Tomas Koudelka, Peter Hoffmann, Jitendra P. Mata, Glyn L. Devlin, Margaret Sunde, Heath Ecroyd, Carl Holt, John A. Carve