Tuesday, February 17, 2009

Online Modern Bio Course and other Bio Resources at Carnegie Mellon!

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Through the OLI project, Carnegie Mellon adds to online education the crucial elements of instructional design grounded in cognitive theory, formative evaluation for students and faculty, and iterative course improvement based on empirical evidence.

A team of biologists, media programmers, and learning experts are creating animations designed to improve understanding of some of the main concepts taught in Modern Biology and Biochemistry.

As supplemental learning resources for the OLI course, we are designing interactive reference pieces to help the students lookup concepts and data they must internalize or use to understand other concepts.

We are developing simulation environments that facilitate multiple, linked representations of concepts to be used in different learning contexts that allow for guided inquiry as well as student directed experimentation and data analysis.

See all their lab demos below:

Protein Purification Practice

This provides the student with a virtual lab demonstration experience where they can be given a unique solution in a beaker and asked to develop a purification scheme to obtain some protein in its pure form. (The classroom version allows the results of their work to be submitted to the instructor for grading).

Protein Folding

This is an experiment to study the effect of temperature on protein stability. Alter the temperature using the slider bar and record the experimental fraction unfolded that is presented in the output box. From this data you need to determine the ∆S and ∆H for unfolding using van't Hoft plot.

Molecular Interactions

Dissociation of Weak Electrolytes

Some molecules are weak electrolytes and exist in a reversible equilibrium between the starting molecule and its dissociated parts. For molecules that are weak electrolytes and act as acids (proton donors), the ratio of the products of the dissociated parts and the parent molecule is a constant (K) in neutral water for each separate molecular structure.

Equilibrium of MO complex formation

Equilibrium state as determined by protein and ligand concentrations: This simulation allows you to explore the equilibrium between free protein, ligand, and the complex, and how ligand concentration affects the equilibrium.

Ligand Binding
Ligand Binding

Membrane Permeability
The introduction of a cell or liposome to the solution places a barrier to the molecules. As three different molecules diffuse to equilibrium in the following simulation, they encounter the lipid bilayer depicted by the horizontal membrane across the center of the stage. Note that one type of molecule passes freely through the lipid bilayer while the second type of molecule only occasionally passes into the membrane and is trapped within. The lipid bilayer is totally impermeable to the third type of molecule. These molecules move through the membranes via passive diffusion.

Osmosis: Isotonic Equilibrium
Cells continually encounter changes in their external ionic environment and will spontaneously respond by attempting to equalize the concentration of ions on the inside and outside of the cell. Because the plasma membrane (lipid bilayer) is significantly less permeable to ions than water, the establishment of an equal concentration of the ions on either side of the membrane is accomplished by the net movement of water toward the higher concentration of ions to reduce the concentration. This movement of water in response to an imbalance of solute (ion) is referred to as osmosis.

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