Multi-Touch Tablets, E-Books, and an Emerging Multi-Coding/Multi-Sensory Theory for Reading Science e-Textbooks: Considering the Struggling Reader

Pavio’s Dual-Coding Theory (1991) and Mayer’s Multimedia Principal (2000) form the foundation for proposing a multi-coding theory centered around Multi-Touch Tablets and the newest generation of e-textbooks to scaffold struggling readers in reading and learning from science textbooks. Using E. O. Wilson’s Life on Earth: An Introduction (2012) as a simulation for our essay, we theorize that text, graphics, interactive elements, and audio represent four distinct encoding schemes. Each of these encoding schemes can be used as separate but mutually supportive scaffolds to assist struggling students in reading and learning with science textbooks.The open access fee for this work was funded through the Texas A&M University Open Access to Knowledge (OAK) Fund

Water Dynamics at Protein Interfaces: Ultrafast Optical Kerr Effect Study

The behavior of water molecules surrounding a protein can have an important bearing on its structure and function. Consequently, a great deal of attention has been focused on changes in the relaxation dynamics of water when it is located at the protein surface. Here we use the ultrafast optical Kerr effect to study the H-bond structure and dynamics of aqueous solutions of proteins. Measurements are made for three proteins as a function of concentration. We find that the water dynamics in the first solvation layer of the proteins are slowed by up to a factor of 8 in comparison to those in bulk water. The most marked slowdown was observed for the most hydrophilic protein studied, bovine serum albumin, whereas the most hydrophobic protein, trypsin, had a slightly smaller effect. The terahertz Raman spectra of these protein solutions resemble those of pure water up to 5 wt % of protein, above which a new feature appears at 80 cm–1, which is assigned to a bending of the protein amide chain

Three Stages of Lysozyme Thermal Stabilization by High and Medium Charge Density Anions

Addition of high and medium charge density anions (phosphate, sulfate, and chloride) to lysozyme in pure water demonstrates three stages for stabilization of the protein structure. The first two stages have a minor impact on lysozyme stability and are probably associated with direct interaction of the ions with charged and partial charges on the protein’s surface. There is a clear transition between the second and third stages; in the case of sodium chloride, disodium sulfate and disodium hydrogen phosphate this is at 550, 210, and 120 mM, respectively. Stabilization of lysozyme can be explained by the free energy required to hydrate the protein as it unfolds. At low ion concentrations, the protein’s hydration layer is at equilibrium with the bulk water. After the transition, bulk water is depleted and the protein is competing for water with the ions. With competition for water between the protein and the ions at higher salt concentrations, the free energy required to hydrate the interior of the protein rises and it is this that stabilizes the protein structure

The interaction of wheat germ agglutinin with keratan from cornea and nasal cartilage

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/21827/1/0000230.pd

Polar or Apolar—The Role of Polarity for Urea-Induced Protein Denaturation

Urea-induced protein denaturation is widely used to study protein folding and stability; however, the molecular mechanism and driving forces of this process are not yet fully understood. In particular, it is unclear whether either hydrophobic or polar interactions between urea molecules and residues at the protein surface drive denaturation. To address this question, here, many molecular dynamics simulations totalling ca. 7 µs of the CI2 protein in aqueous solution served to perform a computational thought experiment, in which we varied the polarity of urea. For apolar driving forces, hypopolar urea should show increased denaturation power; for polar driving forces, hyperpolar urea should be the stronger denaturant. Indeed, protein unfolding was observed in all simulations with decreased urea polarity. Hyperpolar urea, in contrast, turned out to stabilize the native state. Moreover, the differential interaction preferences between urea and the 20 amino acids turned out to be enhanced for hypopolar urea and suppressed (or even inverted) for hyperpolar urea. These results strongly suggest that apolar urea–protein interactions, and not polar interactions, are the dominant driving force for denaturation. Further, the observed interactions provide a detailed picture of the underlying molecular driving forces. Our simulations finally allowed characterization of CI2 unfolding pathways. Unfolding proceeds sequentially with alternating loss of secondary or tertiary structure. After the transition state, unfolding pathways show large structural heterogeneity

Structure and Dynamics of Biological Systems: Integration of Neutron Scattering with Computer Simulation

The combination of molecular dynamics simulation and neutron scattering techniques has emerged as a highly synergistic approach to elucidate the atomistic details of the structure, dynamics and functions of biological systems. Simulation models can be tested by calculating neutron scattering structure factors and comparing the results directly with experiments. If the scattering profiles agree the simulations can be used to provide a detailed decomposition and interpretation of the experiments, and if not, the models can be rationally adjusted. Comparison with neutron experiment can be made at the level of the scattering functions or, less directly, of structural and dynamical quantities derived from them. Here, we examine the combination of simulation and experiment in the interpretation of SANS and inelastic scattering experiments on the structure and dynamics of proteins and other biopolymers

An Analysis of the Possible of Business SImulation Games in Alleviating some of the Reasons for Management Development Faliure

This study is an attempt to identify and analyze some of the reasons for management development program failures and to determine whether the business simulation game can alleviate some of these reasons The findings of the study disclose a number of reasons for management development failure, and that these fall into two categories: administrative and pedagogical. Administrative reasons consist of problems in selection. of participants, lack of organizational support, poorly defined objectives and poor planning, Pedagogical reasons include little opportunity for active participation, retention. of traditional concepts, no provision for individual differences, and lack of originality. The findings further disclose that the business simulation game can alleviate or significantly aid the resolution of all but two of the problems identified The author concludes that the business simulation game provides significant benefits to the corporate management development program, and that companies should make a concerted effort to determine if the objectives of their development effort dictate the use of such a simulation gam