Competency, Experience and Industrial exposure of faculty Members in Public Universities and Collaborating Colleges in Kenya

he success witnessed so far with the Module II Degree Programmes in Kenya’s public universities have led to efforts to expand capacity to absorb more students into public universities. These efforts have included public universities acquiring fully owned satellite campuses in different places/towns, entering into collaboration arrangement with private middle level colleges, adopting various forms/modes of learning facilitation such as holiday, evening or weekend classes, distance, and virtual or e-learning. The Government on its part has declared several middle level colleges to be constituent colleges of different public universities and charters given to more private universities. These rapid changes in public universities often come with their own challenges and may also open up hitherto uncharted horizons or opportunities that could be exploited further. One such challenge is that of the faculty member’s qualification, experience and exposure to enable all these institutions to provide quality education. This paper examines this concern. Faculty members were sampled from public universities, and data obtained as regards their qualification, terms of employment, work expectation and experience, industrial exposure and academic self- development efforts including publications in notable journals. According to the findings made from the study, faculty members in most public universities in Kenya are often middle level ranking with the majority holding Masters Degree qualifications but little else is fully recorded on the attributes that guarantees sustainable availability of competent faculty members where demand for their services is growing by the day. Keywords: Faculty, Experience and Competence

Behavioural cloning of teachers for automatic homework selection

© Springer Nature Switzerland AG 2019. We describe a machine-learning system for supporting teachers through the selection of homework assignments. Our system uses behavioural cloning of teacher activity to generate personalised homework assignments for students. Classroom use is then supported through additional mechanisms to combine these predictions into group assignments. We train and evaluate our system against 50,065 homework assignments collected over two years by the Isaac Physics platform. We use baseline policies incorporating expert curriculum knowledge for evaluation and find that our technique improves on the strongest baseline policy by 18.5% in Year 1 and by 13.3% in Year 2.Cambridge Assessmen

Development and collaborations of a nursing workgroup within a bilateral global medical consortium

We describe the formation of a bilateral nursing workgroup within a global medical consortium of North American and Kenyan healthcare providers and detail our collaboration to advance nursing care, education, and research to improve patient outcomes across a variety of specialties in acute care and community settings in both countries

Development and collaborations of a nursing workgroup within a bilateral global medical consortium

We describe the formation of a bilateral nursing workgroup within a global medical consortium of North American and Kenyan healthcare providers and detail our collaboration to advance nursing care, education, and research to improve patient outcomes across a variety of specialties in acute care and community settings in both countries

Role of water in Protein Aggregation and Amyloid Polymorphism

A variety of neurodegenerative diseases are associated with the formation of amyloid plaques. Our incomplete understanding of this process underscores the need to decipher the principles governing protein aggregation. Most experimental and simulation studies have been interpreted largely from the perspective of proteins: the role of solvent has been relatively overlooked. In this Account, we provide a perspective on how interactions with water affect folding landscapes of A$\beta$ monomers, A$\beta_{16-22}$ oligomer formation, and protofilament formation in a Sup35 peptide. Simulations show that the formation of aggregation-prone structures (N$^*$) similar to the structure in the fibril requires overcoming high desolvation barrier. The mechanism of protofilament formation in a polar Sup35 peptide fragment illustrates that water dramatically slows down self-assembly. Release of water trapped in the pores as water wires creates protofilament with a dry interface. Similarly, one of the main driving force for addition of a solvated monomer to a preformed fibril is the entropy gain of released water. We conclude by postulating that two-step model for protein crystallization must also hold for higher order amyloid structure formation starting from N$^*$. Multiple N$^*$ structures with varying water content results in a number of distinct water-laden polymorphic structures. In predominantly hydrophobic sequences, water accelerates fibril formation. In contrast, water-stabilized metastable intermediates dramatically slow down fibril growth rates in hydrophilic sequences.Comment: 27 pages, 4 figures; Accounts of Chemical Research, 201

The Role of Oligomerization and Cooperative Regulation in Protein Function: The Case of Tryptophan Synthase

The oligomerization/co-localization of protein complexes and their cooperative regulation in protein function is a key feature in many biological systems. The synergistic regulation in different subunits often enhances the functional properties of the multi-enzyme complex. The present study used molecular dynamics and Brownian dynamics simulations to study the effects of allostery, oligomerization and intermediate channeling on enhancing the protein function of tryptophan synthase (TRPS). TRPS uses a set of α/β–dimeric units to catalyze the last two steps of L-tryptophan biosynthesis, and the rate is remarkably slower in the isolated monomers. Our work shows that without their binding partner, the isolated monomers are stable and more rigid. The substrates can form fairly stable interactions with the protein in both forms when the protein reaches the final ligand–bound conformations. Our simulations also revealed that the α/β–dimeric unit stabilizes the substrate–protein conformation in the ligand binding process, which lowers the conformation transition barrier and helps the protein conformations shift from an open/inactive form to a closed/active form. Brownian dynamics simulations with a coarse-grained model illustrate how protein conformations affect substrate channeling. The results highlight the complex roles of protein oligomerization and the fine balance between rigidity and dynamics in protein function

Formation and Growth of Oligomers: A Monte Carlo Study of an Amyloid Tau Fragment

Small oligomers formed early in the process of amyloid fibril formation may be the major toxic species in Alzheimer's disease. We investigate the early stages of amyloid aggregation for the tau fragment AcPHF6 (Ac-VQIVYK-NH2) using an implicit solvent all-atom model and extensive Monte Carlo simulations of 12, 24, and 36 chains. A variety of small metastable aggregates form and dissolve until an aggregate of a critical size and conformation arises. However, the stable oligomers, which are β-sheet-rich and feature many hydrophobic contacts, are not always growth-ready. The simulations indicate instead that these supercritical oligomers spend a lengthy period in equilibrium in which considerable reorganization takes place accompanied by exchange of chains with the solution. Growth competence of the stable oligomers correlates with the alignment of the strands in the β-sheets. The larger aggregates seen in our simulations are all composed of two twisted β-sheets, packed against each other with hydrophobic side chains at the sheet–sheet interface. These β-sandwiches show similarities with the proposed steric zipper structure for PHF6 fibrils but have a mixed parallel/antiparallel β-strand organization as opposed to the parallel organization found in experiments on fibrils. Interestingly, we find that the fraction of parallel β-sheet structure increases with aggregate size. We speculate that the reorganization of the β-sheets into parallel ones is an important rate-limiting step in the formation of PHF6 fibrils

Who is Who in Knowledge Economy in Africa?

This study assesses the knowledge economy (KE) performance of lagging African countries vis-à-vis their frontier counterparts with regard to the four dimensions of the World Bank’s knowledge economy index (KEI). The empirical exercise is for the period 1996-2010. It consists of first establishing leading nations before suggesting policy initiatives that can be implemented by sampled countries depending on identified gaps that are provided with the sigma convergence estimation approach. The following are established frontier knowledge economy countries. (i) For the most part, North African countries are dominant in education. Tunisia is overwhelmingly dominant in 11 of the 15 years, followed by Libya which is a frontier country in two years while Cape Verde and Egypt lead in a single year each. (ii) With the exception of Morocco that is leading in the year 2009, Seychelles is overwhelmingly dominant in ICT. (iii) South Africa also indomitably leads in terms of innovation. (iv) While Botswana and Mauritius share dominance in institutional regime, economic incentives in terms of private domestic credit are most apparent in Angola (8 years), the Democratic Republic of Congo (3 years) and Tanzania, Sierra Leone and Malawi (each leading in one year)

Structure and Dynamics of Amyloid-β Segmental Polymorphisms

Conceived and designed the experiments: WB UH. Performed the experiments: WB. Analyzed the data: WB UH. Contributed reagents/materials/analysis tools: WB UH. Wrote the paper: WB UH.It is believed that amyloid-beta (Aβ) aggregates play a role in the pathogenesis of Alzheimer’s disease. Aβ molecules form β-sheet structures with multiple interaction sites. This polymorphism gives rise to differences in morphology, physico-chemical property and level of cellular toxicity. We have investigated the conformational stability of various segmental polymorphisms using molecular dynamics simulations and find that the segmental polymorphic models of Aβ retain a U-shaped architecture. Our results demonstrate the importance of inter-sheet side chain-side chain contacts, hydrophobic contacts among the strands (β1 and β2) and of salt bridges in stabilizing the aggregates. Residues in β-sheet regions have smaller fluctuation while those at the edge and loop region are more mobile. The inter-peptide salt bridges between Asp23 and Lys28 are strong compared to intra-chain salt bridge and there is an exchange of the inter-chain salt-bridge with intra-chain salt bridge. As our results suggest that Aβ exists under physiological conditions as an ensemble of distinct segmental polymorphs, it may be necessary to account in the development of therapeutics for Alzheimer’s disease the differences in structural stability and aggregation behavior of the various Aβ polymorphic forms.Yeshttp://www.plosone.org/static/editorial#pee