Feminización de la matrícula de educación superior en Puerto Rico

This study represents a collaborative effort among the Educational Research Center of the College of Education at the Rio Piedras Campus, the Higher Education Council, and the UNESCO International Institute for Higher Education in Latin America and the Caribbean. The results, specific to Puerto Rico, contribute to the effort in collecting information on the feminization of the higher education registration rates in Latin America and the Caribbean. The objectives were: 1) gather higher education institutions registration and graduation data of the last 25 years classified bye quinquennia and 2) analyze the data and evaluate possible educational, economic, and social effects in he behavior of the registration, graduation rates, and the workforce, emphasizing their relationship with gender and academic level. The situation in Puerto Rico is compared to other countries and suggestions are provided for future studies.  How to cite: Bonilla-Rodríguez, V., López de Méndez, A., Cintrón-Rodríguez, M., Ramírez-Pagán, S., & Román-Oyola, R. (2005). Feminización de la matrícula de educación superior en Puerto Rico. Cuaderno de Investigación en la Educación, 20, 114-153. Retrieved from https://revistas.upr.edu/index.php/educacion/article/view/16269Este trabajo constituye un esfuerzo colaborativo del Centro de Investigaciones Educativas de la Facultad de Educación del Recinto de Río Piedras. el Consejo de Educación Superior y el Instituto Internacional para la Educación Superior en América Latina y el Caribe de la UNESCO. Los resultdos específicos a Puerto Rico, se suman al esfuerzo por recopilar información sobre la feminización de la matrícula de educación superior en latinoamerica y el Caribe. Los objetivos fueron; 1) recopilar datos sobre matrícula y egresados de instituciones de educación superior de los últimos 25 años clasificados por quinquenio y 2) analizar los datos y evaluar los posibles efectos educativos, económicos y sociales del comportamiento de la matrícula, de los egresados y las ocupaciones de la población, destacando la relación entre éstos, el género y el nivel educativo. Se compara la situación de Puerto Rico con otros países y se proveen  sugerencias para estudios futuros. Cómo citar: Bonilla-Rodríguez, V., López de Méndez, A., Cintrón-Rodríguez, M., Ramírez-Pagán, S., & Román-Oyola, R. (2005). Feminización de la matrícula de educación superior en Puerto Rico. Cuaderno de Investigación en la Educación, 20, 114-153. Recuperado a partir de https://revistas.upr.edu/index.php/educacion/article/view/1626

Fourier transform coupled tryptophan scanning mutagenesis identifies a bending point on the lipid-exposed δM3 transmembrane domain of the Torpedo californica nicotinic acetylcholine receptor

The nicotinic acetylcholine receptor (nAChR) is a member of a family of ligand-gated ion channels that mediate diverse physiological functions, including fast synaptic transmission along the peripheral and central nervous systems. Several studies have made significant advances toward determining the structure and dynamics of the lipid-exposed domains of the nAChR. However, a high-resolution atomic structure of the nAChR still remains elusive. In this study, we extended the Fourier transform coupled tryptophan scanning mutagenesis (FT-TrpScanM) approach to gain insight into the secondary structure of the δM3 transmembrane domain of the Torpedo californica nAChR, to monitor conformational changes experienced by this domain during channel gating, and to identify which lipid-exposed positions are linked to the regulation of ion channel kinetics. The perturbations produced by periodic tryptophan substitutions along the δM3 transmembrane domain were characterized by two-electrode voltage clamp and 125I-labeled α-bungarotoxin binding assays. The periodicity profiles and Fourier transform spectra of this domain revealed similar helical structures for the closed- and open-channel states. However, changes in the oscillation patterns observed between positions Val-299 and Val-304 during transition between the closed- and open-channel states can be explained by the structural effects caused by the presence of a bending point introduced by a Thr-Gly motif at positions 300–301. The changes in periodicity and localization of residues between the closed-and open-channel states could indicate a structural transition between helix types in this segment of the domain. Overall, the data further demonstrate a functional link between the lipid-exposed transmembrane domain and the nAChR gating machinery