| 1. |
- Ferring, Dieter, et al.
(författare)
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Life satisfaction of older people in six European countries: Findings from the European study on adult wellbeing.
- 2004
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Ingår i: European Journal of Ageing. - : Springer Science and Business Media LLC. - 1613-9380 .- 1613-9372. ; 1:1, s. 15-25
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Tidskriftsartikel (refereegranskat)abstract
- The European Study on Adult Well-being (ESAW), funded by the European Union, was conducted during 2002 and 2003 in Austria, Italy, Luxembourg, The Netherlands, United Kingdom and Sweden. The aim of the interdisciplinary study was the conceptual clarification and the identification of factors contributing to life satisfaction for older people. Five key components were included in the study: (1) physical health and functional status; (2) self-resources; (3) material security; (4) social support resources; and (5) life activity. A representative population of adults aged 50–90 years living independently (not institutionalised) was selected in each participating country, and the actual sample size came very close to the target of 2,000, ranging from 1,854 to 2,417. The total European sample comprised 12,478 respondents. In this paper, mean differences in general and domain-specific life satisfaction between the six countries including age groups and gender are reported and discussed with respect to contextual national characteristics. In general the findings showed a high level in all chosen indicators of life satisfaction across the six countries. National differences depended on the domain under consideration, but the results showed in general that The Netherlands, United Kingdom, Luxembourg and Austria had higher values of life satisfaction compared to Sweden and Italy.
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| 2. |
- Koivula, Anu, et al.
(författare)
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The active site of cellobiohydrolase Cel6A from Trichoderma reesei: the roles of aspartic acids D221 and D175.
- 2002
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Ingår i: J Am Chem Soc. - : American Chemical Society (ACS). - 0002-7863 .- 1520-5126. ; 124:34, s. 10015-24
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Tidskriftsartikel (refereegranskat)abstract
- Trichoderma reesei cellobiohydrolase Cel6A is an inverting glycosidase. Structural studies have established that the tunnel-shaped active site of Cel6A contains two aspartic acids, D221 and D175, that are close to the glycosidic oxygen of the scissile bond and at hydrogen-bonding distance from each other. Here, site-directed mutagenesis, X-ray crystallography, and enzyme kinetic studies have been used to confirm the role of residue D221 as the catalytic acid. D175 is shown to affect protonation of D221 and to contribute to the electrostatic stabilization of the partial positive charge in the transition state. Structural and modeling studies suggest that the single-displacement mechanism of Cel6A may not directly involve a catalytic base. The value of (D2O)(V) of 1.16 +/- 0.14 for hydrolysis of cellotriose suggests that the large direct effect expected for proton transfer from the nucleophilic water through a water chain (Grotthus mechanism) is offset by an inverse effect arising from reversibly breaking the short, tight hydrogen bond between D221 and D175 before catalysis.
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