Integrating organizational, social, and individual perspectives in Web 2.0-based workplace e-learning

From the issue entitled 'Special Issue: Emerging Social and Legal Aspect'E-learning is emerging as a popular approach of education in the workplace by virtue of its flexibility to access, just-in-time delivery, and cost-effectiveness. To improve social interaction and knowledge sharing in e-learning, Web 2.0 is increasingly utilized and integrated with e-learning applications. However, existing social learning systems fail to align learning with organizational goals and individual needs in a systemic way. The dominance of technology-oriented approaches makes elearning applications less goal-effective and poor in quality and design. To solve the problem, we address the requirement of integrating organizational, social, and individual perspectives in the development of Web 2.0 elearning systems. To fulfill the requirement, a key performance indicator (KPI)-oriented approach is presented in this study. By integrating a KPI model with Web 2.0 technologies, our approach is able to: 1) set up organizational goals and link the goals with expertise required for individuals; 2) build a knowledge network by linking learning resources to a set of competences to be developed and a group of people who learn and contribute to the knowledge network through knowledge creation, sharing, and peer evaluation; and 3) improve social networking and knowledge sharing by identifying each individual's work context, expertise, learning need, performance, and contribution. The mechanism of the approach is explored and elaborated with conceptual frameworks and implementation technologies. A prototype system for Web 2.0 e-learning has been developed to demonstrate the effectiveness of the approach. © Springer Science + Business Media, LLC 2009.postprin

Professional Learning Communities as drivers of educational change: the case of Learning Rounds

Many researchers claim that there is a compelling weight of evidence for the effectiveness of PLCs in promoting teachers’ learning and pupil achievement. However, others raise fundamental questions about their nature and purpose. Some of the uncertainties about the nature and purpose of PLCs relate to the ways in which the macro-context of neo-liberalism has shaped the practices of PLCs in particular ways. The fundamental questions raised about PLCs relate to the type of change they are intended to produce, the model of community they are based on and whether the right conditions and skills are in place for them to contribute to change. Some researchers argue that we need to pay more attention to shortcomings within existing PLCs and their internal dynamics. Others argue that little research focuses on the specific interactions of teachers inside PLCs. The research reported here goes ‘inside the teacher community’ of Learning Rounds to explore what the shortcomings of some examples of this model in practice add to what we know about how to assist PLCs to produce change in education

Evolution of Hydrogen-Bond Networks in Protonated Water Clusters H⁺(H₂O)_<i>n</i> (<i>n</i> = 1 to 120) Studied by Cryogenic Ion Mobility-Mass Spectrometry

Cryogenic (80 K) ion mobility-mass spectrometry (cryo-IM-MS) is employed to study structural transitions of protonated water clusters in both the small, H⁺(H₂O)_<i>n</i> (<i>n</i> = 1 to 30), and large, (<i>n</i> = 31 to ∼120), size regions. In agreement with previous studies, we find compelling evidence of regions of uniform cluster decay in the small size region, accompanied by sharp transition points whereby the loss of a single water monomer induces a different H-bonding motif. The investigation of the isomeric distribution of each species at 80 K reveals experimental evidence supporting the notion that H⁺(H₂O)_<i>n</i> (<i>n</i> = 6) is the smallest system to possess both Eigen- (H₃O⁺) and Zundel- (H₅O₂⁺) centered structures. Cryo-IM-MS is particularly well-suited for studying clusters in the large size region, for which previous spectroscopic experimental studies are scarce

Water-Mediated Dimerization of Ubiquitin Ions Captured by Cryogenic Ion Mobility-Mass Spectrometry

The dynamics, structures, and functions of most biological molecules are strongly influenced by the nature of the peptide’s or protein’s interaction with water. Here, cryogenic ion mobility-mass spectrometry studies of ubiquitin have directly captured a water-mediated protein–protein binding event involving hydrated, noncovalently bound dimer ions in solution, and this interaction has potential relevance to one of the most important protein–protein interactions in nature. As solvent is removed, dimer ions, viz. [2 M + 14H]¹⁴⁺, can be stabilized by only a few attached water molecules prior to dissociation into individual monomeric ions. The hydrophobic patch of ubiquitin formed by the side chains of Leu-8, Ile-44, and Val-70 meet all the necessary conditions for a protein–protein binding “hot spot,” including the requirement for occlusion of water to nearby hydrophilic sites, and it is suggested that this interaction is responsible for formation of the hydrated noncovalent ubiquitin dimer

From Solution to the Gas Phase: Factors That Influence Kinetic Trapping of Substance P in the Gas Phase

Substance P (RPKPQQFFGLM-NH₂) [M + 3H]³⁺ ions have been shown to exist as two conformers: one that is kinetically trapped and one that is thermodynamically more stable and therefore energetically preferred. Molecular dynamics (MD) simulations suggested that the kinetically trapped population is stabilized by interactions between the charge sites and the polar side chains of glutamine (Q) located at positions 5 and 6 and phenylalanine (F) located at positions 7 and 8. Here, the individual contributions of these specific intramolecular interactions are systematically probed through site-directed alanine mutations of the native amino acid sequence. Ion mobility spectrometry data for the mutant peptide ions confirm that interactions between the charge sites and glutamine/phenylalanine (Q/F) side chains afford stabilization of the kinetically trapped ion population. In addition, experimental data for proline-to-alanine mutations at positions 2 and 4 clearly show that interactions involving the charge sites and the Q/F side chains are altered by the cis/trans orientations of the proline residues and that mutation of glycine to proline at position 9 supports results from MD simulations suggesting that the C-terminus also provides stabilization of the kinetically trapped conformation

Unfolding of Hydrated Alkyl Diammonium Cations Revealed by Cryogenic Ion Mobility-Mass Spectrometry

Hydration of the ammonium ion plays a key role in determining the biomolecular structure as well as local structure of water in aqueous environments. Experimental data obtained by cryogenic ion mobility-mass spectrometry (cryo-IM-MS) show that dehydration of alkyl diammonium cations induces a distinct unfolding transition at a critical number of water molecules, <i>n</i> = 21 to 23, <i>n</i> = 24 to 26, and <i>n</i> = 27 to 29, for 1,7-diaminoheptane, 1,8-diaminooctane, and 1,10-diaminodecane, respectively. Results are also presented that reveal compelling evidence for unique structural transitions of hydrated ammonium ions associated with the development of the hydrogen-bond network around individual charged groups. The ability to track the evolution of structure upon stepwise dehydration provides direct insight into the intricate interplay between solvent–molecule interactions that are responsible for defining conformations. Such insights are potentially valuable in understanding how ammonium ion solvation influences conformation(s) of larger biomolecules