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1.
Can J Public Health ; 90(2): 99-103, 1999.
Artigo em Francês | MEDLINE | ID: mdl-10349215

RESUMO

The aim of this paper is to explore public health professionals' perceptions regarding two dimensions of the new health promotion movement: the ecological approach and the principle of community participation. Data were collected by focus-groups of public health professionals (n = 22) in one Public Health Directorate in Québec. Results indicate a fair degree of integration of these two dimensions into the respondents' professional practice. However, limitations related to the work environment and to the theoretical underpinnings of these two components might impede the respondents' ability to integrate them into their practice.


Assuntos
Ecologia , Promoção da Saúde/métodos , Prática de Saúde Pública , Grupos Focais , Humanos , Pessoa de Meia-Idade , Modelos Teóricos , Quebeque
2.
Can Nurse ; 94(5): 36-42, 1998 May.
Artigo em Francês | MEDLINE | ID: mdl-9923211

RESUMO

The public's diversified language profile means that nursing practice must adjust to provide the same quality of care to all clients, no matter what language they speak. To improve quality and quantity of information exchanged in the nurse-client-interpreter triangle, the authors have investigated the type of information likely to be filtered and studied the various factors underlying the interpreter's choice to filter information. The authors also analyzed the values interpreters assign to information and the factors that form the background for filtering, including mistrust. The authors suggest adequately preparing interpreters; using interpreters' expertise; and developing an appropriate training program for intercultural interpreters to enable them to better function within health care institutions.


Assuntos
Comunicação , Multilinguismo , Relações Enfermeiro-Paciente , Enfermagem Transcultural/métodos , Tradução , Diversidade Cultural , Humanos
3.
Int J Pept Protein Res ; 47(1-2): 9-19, 1996.
Artigo em Inglês | MEDLINE | ID: mdl-8907494

RESUMO

alpha- and betaB2-Crystallin are the major proteins in the mammalian lens. Each of these crystallins has short, flexible terminal extensions from its domain core; the two alpha-crystallin subunits have C-terminal extensions of eight and ten amino acids whilst betaB2-crystallin has N- and C-terminal extensions of 15 and 11 amino acids, respectively. The solution conformations of these chemically synthesised extensions have been examined by two-dimensional 1H NMR spectroscopy. The N-terminal extension of betaB2-crystallin and the C-terminal extensions of alpha-crystallin adopt little ordered structure. In the membrane-mimicking solvent trifluoroethanol, the alpha-crystallin extensions are also unstructured. In contrast, the C-terminal extension of betaB2-crystallin in water has a structural preference towards turn-like structures, creating a hydrophobic region involving G198, F200 and P202. In the lens, the C-terminal extension of betaB2-crystallin is the only one of these extensions that interacts to any large extent with other crystallins. The structural preference of the C-terminal extension of betaB2-crystallin may therefore have implications for the role of this extension in crystallin-crystallin interactions.


Assuntos
Cristalinas/química , Fragmentos de Peptídeos/química , Animais , Bovinos , Espectroscopia de Ressonância Magnética , Conformação Proteica , Prótons , Soluções
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