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Articles 1 - 2 of 2
Full-Text Articles in Life Sciences
Improved Student Learning Through A Faculty Learning Community: How Faculty Collaboration Transformed A Large-Enrollment Course From Lecture To Student Centered, Emily R. Elliott, Robert D. Reason, Clark R. Coffman, Eric J. Gangloff, Jeffrey R Raker, Jo Anne Powell-Coffman, Craig A. Ogilvie
Improved Student Learning Through A Faculty Learning Community: How Faculty Collaboration Transformed A Large-Enrollment Course From Lecture To Student Centered, Emily R. Elliott, Robert D. Reason, Clark R. Coffman, Eric J. Gangloff, Jeffrey R Raker, Jo Anne Powell-Coffman, Craig A. Ogilvie
Chemistry Faculty Publications
Undergraduate introductory biology courses are changing based on our growing understanding of how students learn and rapid scientific advancement in the biological sciences. At Iowa State University, faculty instructors are transforming a second-semester large-enrollment introductory biology course to include active learning within the lecture setting. To support this change, we set up a faculty learning community (FLC) in which instructors develop new pedagogies, adapt active-learning strategies to large courses, discuss challenges and progress, critique and revise classroom interventions, and share materials. We present data on how the collaborative work of the FLC led to increased implementation of active-learning strategies and …
Method For Measuring The Unbinding Energy Of Strongly-Bound Membrane-Associated Proteins, Elisa La Bauve, Briana C. Vernon, Dongmei Ye, David M. Rogers, Cathryn M. Siegrist, Bryan D. Carson, Susan B. Rempe, Aihua Zheng, Margaret Kielian, Andrew P. Shreve, Michael S. Kent
Method For Measuring The Unbinding Energy Of Strongly-Bound Membrane-Associated Proteins, Elisa La Bauve, Briana C. Vernon, Dongmei Ye, David M. Rogers, Cathryn M. Siegrist, Bryan D. Carson, Susan B. Rempe, Aihua Zheng, Margaret Kielian, Andrew P. Shreve, Michael S. Kent
Chemistry Faculty Publications
We describe a new method to measure the activation energy for unbinding (enthalpy ΔH*u and free energy ΔG*u) of a strongly-bound membrane-associated protein from a lipid membrane. It is based on measuring the rate of release of a liposome-bound protein during centrifugation on a sucrose gradient as a function of time and temperature. The method is used to determine ΔH*u and ΔG*u for the soluble dengue virus envelope protein (sE) strongly bound to 80:20 POPC:POPG liposomes at pH 5.5. ΔH*u is determined from the Arrhenius equation whereas ΔG*u is …