Valoración del practicum. Aportaciones de los/las estudiantes en relación al practicum de psicología de la Universidad de Girona (2006-2009)

El siguiente trabajo es una valoración de carácter cualitativo sobre el practicum de psicología realizada por los estudiantes que han acabado el practicum el último año de licenciatura. Trata de explorar los siguientes aspectos: objetivos del practicum, tipos de tareas realizadas, tutorías, valoración sobre la calidad de los centros, organización del practicum y seminario de ética. Se tendrán en cuenta 5 ámbitos que abarcan los Centros de practicum de psicología: intervención psicosocial en servicios especializados, clínica, organizaciones, educación y practicum de investigación

Une Innovation didactique basée sur les nanotechnologies au lycée: quels effets sur la dynamique professionnelle des enseignants?

Une nouvelle stratégie éducative a associé durant trois ans (2006-2009), au sein d’un lycée toulousain, enseignants du secondaire et chercheurs en sciences (CNRS-LAAS) et sciences humaines (ERT 64-GRIDIFE). Dans une classe de Terminale Scientifique, elle permet de combiner enseignement scientifique (mathématiques, physique-chimie, Sciences de la Vie et de la Terre) et enseignement aux « humanités » (philosophie, histoire-géographie-Éducation Civique, Juridique et Sociale (ECJS), anglais). Cette ingénierie d’éducation citoyenne des sciences repose sur l’enseignement des nanotechnologies. Ces dernières touchent de nombreux secteurs d’application et sont appelées à connaître un fort développement dans la société, engendrant de ce fait, de nombreux bouleversements en matière de développements économiques et industriels mais aussi de questionnements sur les relations entre sciences, technologies et société1. L’ingénierie d’éducation citoyenne aux sciences met l’accent sur la complémentarité entre formation scientifique et éthique pour éduquer les futurs citoyens à faire face à l’incertitude liée aux technosciences et leur impact sur la société (Désautels, 2002 ; Bensaude-Vincent, 2009)

Destabilizing Mutations Alter the Hydrogen Exchange Mechanism in Ribonuclease A

The effect of strongly destabilizing mutations, I106A and V108G of Ribonuclease A (RNase A), on its structure and stability has been determined by NMR. The solution structures of these variants are essentially equivalent to RNase A. The exchange rates of the most protected amide protons in RNase A (35ºC), the I106A variant (35ºC), and the V108G variant (10ºC) yield stability values of 9.9, 6.0, and 6.8 kcal/mol, respectively, when analyzed assuming an EX2 exchange mechanism. Thus, the destabilization induced by these mutations is propagated throughout the protein. Simulation of RNase A hydrogen exchange indicates that the most protected protons in RNase A and the V108G variant exchange via the EX2 regime, whereas those of I106A exchange through a mixed EX1 1 EX2 process. It is striking that a single point mutation can alter the overall exchange mechanism. Thus, destabilizing mutations joins high temperatures, high pH and the presence of denaturating agents as a factor that induces EX1 exchange in proteins. The calculations also indicate a shift from the EX2 to the EX1 mechanism for less protected groups within the same protein. This should be borne in mind when interpreting exchange data as a measure of local stability in less protected regions

Distinct Unfolding and Refolding Pathways of Ribonuclease A Revealed by Heating and Cooling Temperature Jumps

Heating and cooling temperature jumps (T-jumps) were performed using a newly developed technique to trigger unfolding and refolding of wild-type ribonuclease A and a tryptophan-containing variant (Y115W). From the linear Arrhenius plots of the microscopic folding and unfolding rate constants, activation enthalpy (ΔH#), and activation entropy (ΔS#) were determined to characterize the kinetic transition states (TS) for the unfolding and refolding reactions. The single TS of the wild-type protein was split into three for the Y115W variant. Two of these transition states, TS1 and TS2, characterize a slow kinetic phase, and one, TS3, a fast phase. Heating T-jumps induced protein unfolding via TS2 and TS3; cooling T-jumps induced refolding via TS1 and TS3. The observed speed of the fast phase increased at lower temperature, due to a strongly negative ΔH# of the folding-rate constant. The results are consistent with a path-dependent protein folding/unfolding mechanism. TS1 and TS2 are likely to reflect X-Pro114 isomerization in the folded and unfolded protein, respectively, and TS3 the local conformational change of the β-hairpin comprising Trp115. A very fast protein folding/unfolding phase appears to precede both processes. The path dependence of the observed kinetics is suggestive of a rugged energy protein folding funne

Towards economic and monetary union: changing trends in payment systems for new european members

The objective of this paper is precisely to study the evolution of payment systems within the accession countries between 1996 and 2003 and compare them with those of the E.U. and the Eurozone countries

European payment system and monetary union

We make a comparative study of payment systems for E.U. -fifteen countries for the 1996-2002 period. Special attention is paid to the introduction of the new European single currency. The overall trend in payments is for a move from cash to noncash payment instruments, although electronic instruments are not widely used yet. We find a significant impact from the introduction of the new banknotes and coins on card use