[Ressenya del llibre Rediscovering geography: new relevance for science and society, de Rediscovering Geography Committee, National Research Council]

El llibre ressenyat pretén ser una síntesi i una avaluació de la situació de la geografia als Estats Units. Estructurat en vuit capítols, els sis primers són una anàlisi de diversos aspectes de la geografia i els dos últims expliquen quina estratègia hauria de portar-se a terme per enfortir el paper de la geografia en el món acadèmic i en la societat en general

Didactics–promoting collaborative work and personal learning environment. Critical, creative and autonomous roles in a competitive society

School has evolved from a place where knowledge is provided to a place where learners are helped to develop their professional and social skills. Consequently, education must evolve through big challenges in order to face the changes of society in the XXIst century

Pressure-jump-induced kinetics reveals a hydration dependent folding/unfolding mechanism of ribonuclease A

Pressure-jump (p-jump)-induced relaxation kinetics was used to explore the energy landscape of protein folding/unfolding of Y115W, a fluorescent variant of ribonuclease A. Pressure-jumps of 40MPa amplitude (5ms dead-time) were conducted both to higher (unfolding) and to lower (folding) pressure, in the range from 100 to 500MPa, between 30 and 50°C. Significant deviations from the expected symmetrical protein relaxation kinetics were observed. Whereas downward p-jumps resulted always in single exponential kinetics, the kinetics induced by upward p-jumps were biphasic in the low pressure range and monophasic at higher pressures. The relative amplitude of the slow phase decreased as a function of both pressure and temperature. At 50°C, only the fast phase remained. These results can be interpreted within the framework of a two-dimensional energy surface containing a pressure- and temperature-dependent barrier between two unfolded states differing in the isomeric state of the Asn-113–Pro-114 bond. Analysis of the activation volume of the fast kinetic phase revealed a temperature-dependent shift of the unfolding transition state to a larger volume. The observed compensation of this effect by glycerol offers an explanation for its protein stabilizing effect