Adventures in flipping a course: how fiscal constraints, student complaints and colleague skepticism helped me achieve my goal

Many of us have heard about the “flipped” classroom, where students first learn about a subject outside of the classroom, and class time is used for application/group work. And we’ve probably all heard of the power of active learning. But logistics, resource limitations and student attitudes can often appear insurmountable obstacles to adopting such strategies. After participants brainstorm the diverse challenges to flipping a course, I’ll describe my 4-year “adventure” in flipping an introductory microbiology course. Created as part of a curriculum restructuring, this new course was designed to have students “learn by doing”. However beyond the laboratory exercises, the reality of limited resources, support, time and much higher enrolment than forecast, all became perceived obstacles to accomplishing these goals. I will describe how, through an iterative process, and relying on diverse collaborations beyond the bounds of the department and university, we arrived at a scalable course design that requires little to no additional resources, is designed to promote student success and engagement, and can be undertaken by even the most skeptical future instructor. The course begins gently, with a few weeks of traditional lecture combined with non-graded active learning group work in the classroom, and traditional laboratory exercises. The students then transition to a fully flipped experience, with class/laboratory sessions used for group work/peer instruction, and a case study that includes laboratory investigations. Following presentation of this case study, participants will reflect on, and share, possible strategies to resolve at least some of the challenges with their own courses

Videos in STEM courses: A 21st century tool in higher education

The call for actively engaging students in the STEM classroom has increased to a clamour in recent years – in the field of biology, this is reflected through the call for student-centered learning in the 2011 AAAS Vision and Change document (http://visionandchange.org). The flipped classroom is arguably the most student-centered and interactive of the various active learning approaches. Central to this type of course are the instructional videos that students watch before class. While the concept of a flipped class may be of interest to many, the need to create these videos is often the perceived obstacle that prevents adoption of a flipped approach. Outside of the flipped classroom, there are a variety of other uses for instructor-created videos. In this presentation, we will discuss how we have incorporated instructional videos, lecture capture and screencasts in our flipped, blended and non-flipped courses. Participants will learn how simple these videos are to make and disseminate and will hear about the various types and uses of instructional videos. They will have the opportunity to debate the pros and cons of possibly the most controversial of instructional videos: lecture capture. Many dental and medical schools have been recording their lectures for years, yet this practice is not common in STEM education: why? The session will end with participants brainstorming possible uses for their own courses. In a follow-up workshop, we will provide hands-on experience to help participants make their own short instructional videos

Identification of Residues Involved in Catalytic Activity of the Inverting Glycosyl Transferase WbbE from Salmonella enterica Serovar Borreze

Synthesis of the O:54 O antigen of Salmonella enterica is initiated by the nonprocessive glycosyl transferase WbbE, assigned to family 2 of the glycosyl transferase enzymes (GT2). GT2 enzymes possess a characteristic N-terminal domain, domain A. Based on structural data from the GT2 representative SpsA (S. J. Charnock and G. J. Davies, Biochemistry 38:6380–6385, 1999), this domain is responsible for nucleotide binding. It possesses two invariant Asp residues, the first forming a hydrogen bond to uracil and the second coordinating a Mn(2+) ion. Site-directed replacement of Asp41 (D41A) of WbbE, the analogue of the first Asp residue of SpsA, revealed that this is not required for activity. WbbE possesses three Asp residues near the position analogous to the second conserved residue. Whereas D95A reduced WbbE activity, activity in D93A and D96A mutants was abrogated, suggesting that either D93 or D96 may coordinate the Mn(2+) ion. Our studies also identified a C-terminal region of sequence conservation in 22 GT2 members, including WbbE. SpsA was not among these. This region is characterized by an ED(Y) motif. The Glu and Asp residues of this motif were individually replaced in WbbE. E180D in WbbE had greatly reduced activity, and an E180Q replacement completely abrogated activity; however, D181E had no effect. E180 is predicted to reside on a turn. Combined with the alignment of the motif with potential catalytic residues in the GT2 enzymes ExoM and SpsA, we speculate that E180 is the catalytic residue of WbbE. Sequence and predicted structural divergence in the catalytic region of GT2 members suggests that this is not a homogeneous family