DYLAN AUDETTE, PH.D.

BIOLOGY AND CHEMISTRY EDUCATOR

(302) 312-5755 – Dylanaudette@gmail.com – www.dylanaudette.com

Profile

Innovative educator who designs and implements instruction to ensure students are engaged learners who develop the knowledge, skills, and understanding of the sciences. Strategic planner who intentionally establishes an inclusive learning environment through real world, problem-based learning, research-based instructional practices, and authentic and varied assessments which promotes student success and agency, including those underrepresented in the sciences.  Dedicated and collaborative mentor and colleague who prioritizes student growth and departmental success through giving personal attention, demonstrating passion for learning, and working with teams to meet goals.

EDUCATION

Teaching Experience

Service to the University and Professional Societies

Selected Honors and Awards

 

Presentations – Pedagogy and EducatioNal Research

Publications

 

 

Professional Affiliations

Professional References

Mark Overmyer-Velázquez, PhD
University Campus Director, UConn Hartford
Professor of History and Latino & Latin American Studies
Mark.Velazquez@uconn.edu

John Cooley, PhD
Assistant Professor in Residence of Ecology and Evolutionary Biology
john.cooley@uconn.edu
959.200.3908

Christine Mosman
Associate Director of Student Services, UConn Hartford Regional Campus
Christine.mosman@uconn.edu
959.200.3836

John R. Jungck, Ph.D

Former Administrator and Mentor: Interdisciplinary Sciences Learning Laboratory

Professor of Biological Sciences and Mathematics, University of Delaware
jungck@udel.edu
(302) 831-6400

 

DYLAN AUDETTE, PH.D.

BIOLOGY AND CHEMISTRY EDUCATOR

(302) 312-5755 – Dylan.audette@uconn.edu [DA1] – www.dylanaudette.com

Appendix Contents:

A1:	Provost’s commendation for excellence in teaching, Spring Semester 2019 and Fall Semester 2018
A2:	Exam Revision Assignments: overview, exemplar, and ongoing research
A3:	Malate Dehydrogenase Course-Based Undergraduate Research Experience, overview, exemplars, and ongoing research

 

APPENDIX A1: PROVOST’S COMMENDATION FOR EXCELLENCE IN TEACHING, SPRING SEMESTER 2019 AND FALL SEMESTER 2018

Following the conclusion of each semester the office of UCONN’s Provost sends out commendations for excellence in teaching. The Provost recognize professors who have received exemplary evaluations from their students in their end of semester anonymous evaluations. I received awards for my performance in the fall semester of 2018 and the spring semesters of 2019. The commendation letters are presented on the following pages.

 

 

Appendix A2: Exam Revision Assignments: overview, exemplar, and ongoing research

Overview:

Exam revision assignment that encourages students to review course topics they had not mastered on mid-term exams.

Why these were necessary:

My students’ insufficient mastery of course learning objectives surprised me when I first assessed my BIOL1107 course in the spring of 2018. My students’ exam performance drastically underperformed my expectations compared to the work that they had completed in the classroom. Two things became clear after talking to some of my students and surveying the class in the class following the exam:

1.       Students expected that a small amount of studying would be sufficient to earn a passing grade on a midterm exam. In a poll, ~75% or responders thought that they should spend less than 6 hours studying course content that was covered in seven seventy-five-minute courses.

2.       Students did not know how to study. When asked to rank the methods used for studying my students overwhelmingly reported that reading the textbook and rereading notes were the most-used techniques.

It was apparent that my students would need to learn how to learn and experience the process of preparing for an exam in order to meet the high standards that I set for my course. I developed these assignments to cause students to review unmastered objectives and reflect on what they might have done to master this content originally. I hoped that this skill would cause students to increase their preparation for future exams and increase their mastery of learning objectives.

Assignment Description

Students were provided with detailed formative feedback on short answer problems and a key of the multiple-choice responses. Each of these problems indicated which course learning objective was being assessed by that problem. Students were asked to review each problem that they had not earned full credit for on the preceding exam.

For each incorrect problem they were asked to submit a mini essay that:

1.       Described why the correct answer was correct (with a sufficient level of detail to show that they now fully understood the associated learning objective).

2.       Describe what was incorrect about their response

3.       Reflect on how they might have prepared for this topic during the exam

4.       (Exams 2 and 3 only) In subsequent exams students were also asked to reflect on how they had implemented their learning plan from the preceding revision.

If students demonstrated mastery of a topic they received a 50% return of lost exam credit. Students submitted work of varying qualities, so most did not earn full credit back initially. These students were invited to re-submit a new version of their work that was of sufficient quality.  Through this iterative process I saw students’ reported study habits grow, though many students struggled with just how much growth and effort was required of them to catch-up to their peers who arrived prepared to meet course standards.

Current Research

I have been collecting data to publish the efficacy of this practice through the 2019 Spring and Fall semesters. Results look promising and it appears that students who revised an item are more likely to master this same learning objective on a final exam than peers from a control group who were not able to revise that item.

Example work

An example exemplar exam revision follows beginning on the next page, reproduced with the student’s consent.

Example Exam Revision, submitted by one of Professor Audette’s BISC 1107 during the fall of 2019

In this assignment students were asked to revise incorrect answers from their last exam and reflect on how they should better prepare for future exams.

The graph to the left compares the change in free energy over the course of a reaction. One line shows the catalyzed reaction (with an enzyme), the other shows the uncatalyzed reaction. What is the activation energy for the reaction that occurs without an enzyme?

In general, activation energy is the difference in free energy between reactants and transition states. ∆G is the change in energy between products and reactants. The graph is exergonic and releases energy. The catalyzed reaction is the reaction that is catalyzed (sped up) by a biocatalytic process, which in this case is an enzyme. The orange line is the catalyzed reaction. The peak of the catalyzed reaction is at 300 Kcal/M and the initial state of the blue line’s reaction is 200 Kcal/M. Based on the definition of activation energy, the blue line’s initial state of 200 Kcal/M must be subtracted from 300 Kcal/M, giving an answer of 100 Kcal/M. My answer, c was incorrect because I had not realized that the curve with the lower transition state was the one that was catalyzed by an enzyme.

In the question above, this student did not correctly apply the concept of activation energy on her exam. This can be a tricky concept; it is defined as: The difference in energy of the reactant and transition state. However, many students have a misconception that this results between two other points on the graphs above. This is best exemplified when comparing the transition states of exergonic and endergonic reactions, which the student does in her drawing to the right. On the exam this question also asked students to differentiate between a catalyzed and uncatalyzed reaction, and the student relates this cartelization to the speeding up of the reaction and a decrease in the activation energy in her plot. This response earned full credit for content revision, though I asked her to spend some time focusing on reflecting on her studying practices in future revisions.

A better example of reflection is shown below by a student who originally struggled to describe why cells would be required to perform anaerobic respiration (ans: a lack to O2 leads to the inability to recycle NADH to NAD+):

Question 8 / Correct Answer - D (There is insufficient NAD+ to complete glycolysis)

This question was tricky for me, due to the fact that I didn’t put enough effort into studying why lactic acid fermentation occurs. I have since rewatched the parts of the lectures on this topic, and feel better about this question now rather than when I was taking the test. I thought that human cells will perform anaerobic respiration through lactic acid fermentation if there is insufficient ATP to initiate glycolysis. However, I now understand that in order for glycolysis to occur, we need a ready supply of oxidized electron carriers (NAD+). Without them, all processes will become backed up, which is why they need to be available in the beginning process, glycolysis.

I really feel like I am on the brink of hitting my stride in this class. After meeting with you twice and getting extra help from the biology tutor Shanell, my confidence is going up. I just have to practice executing the material that I study before the exam coming up. I have the studying aspect down pretty much, but it’s the application of those long hours spent studying where I am still working on. I promised myself before college started that I would give 100%effort no matter what, and I feel that my effort is close to paying off. It is taking longer than I like, but I am getting there.

Appendix A3: Malate Dehydrogenase Course-Based Undergraduate Research Experience, overview, exemplars, and ongoing research

Overview:

Created a course-based undergraduate research experience (CURE) where each student posed a hypothesis about the function of an amino acid in the Malate Dehydrogenase enzyme, then designed, created, and characterized mutant enzymes to test their hypotheses.

Antebellum laboratory exercises:

The introductory biology labs I inherited in the spring of 2018 broadly lacked investigation and often even experimentation. Several of the labs asked only that students view pre-dissected specimens and posters showing the anatomy of diverse structures and commit them to memory.

Introductory laboratories are the place many students first encounter science, and the antebellum laboratories we provided for our students told them that science was about rote memorization and recall. An ideal laboratory would encourage students to craft hypothesis and experiment, but such activities are difficult to standardize and require time, materials, and funding we did not yet have.

Development of a Course-based Undergraduate Research Experience

By the summer of 2019 I had secured internal funding to sustainably expand the BIOL1107 laboratories. I purchased iPads for students to document their work, analyze their results, and create presentations. The Storrs campus donated used but serviceable UV-spectrometers when they were updating their labs. I purchased centrifuges, micropipettes, glassware and consumables.

Simultaneously I connected with the Malate Dehydrogenase CURE Community, an extant group of educators and researchers who had developed protocols to mutate, produce, and characterize novel Malate Dehydrogenase (MDH) proteins. While most biochemical research is prohibitively expensive to perform in a teaching laboratory, MDH catalyzes a reaction that can be viewed using a simple UV spec by measuring the concentration of a reactant. UConn Hartford’s Campus Director funded my teaching-release to develop a full lab course curriculum during the second summer session. The project I develop consisted of the following activities:

1.       Students were introduced to standard curves and several standard lab techniques over 3 weeks.

2.       Students learned about MDH and performed phylogenetic analysis of its sequence to identify regions of interest. Students learn to use the PyMol molecular visualization tool to model protein structures.

3.       Students used their results from the previous week and their understanding of protein folding from lecture to pick a phylogenetically conserved amino acid in MDH and form a hypothesis about how the enzyme might be affected by targeted mutation. Students then designed constructs to perform site-directed mutagenesis.

4.       Students then spent 2 weeks learning to read several scientific papers about MDH and constructing a presentation proposing their hypothesis for study. Students used their protein models and phylogenetic analysis as supporting data. While students prepared their presentations, my collaborators performed site-directed mutagenesis to produce mutants for my students.

5.       Students presented their work and received formative feedback about how to improve their hypothesis and supporting data before their final presentation.

6.       We completed several standard laboratory exercises while I prepared their proteins. I expressed their novel MDH mutants and purified their proteins bi nickel column chromatography. In future semester students will perform this step as well, but I lacked a sufficiently well designed and safe protocol to allow students to complete this work this semester.

7.       Following purification of their proteins, students spent two weeks performing measurements of enzyme specific activity to support their hypothesis, followed by a presentation of their work and conclusions.

These experiments were flanked by pre and post-test assessments of scientific identity and practice, and an analysis of the outcomes of this pedagogical research is underway. On the following page please find an annotated example student report.

 

Example Slides from a MDH Cure Final Presentation, submitted by one of Professor Audette’s BISC 1107 during the fall of 2019. Example slides are presented with some commentary.

Figure1: This group generally provided a strong presentation, but they had some sequencing issues with their background section. They began their presentation with MDH before describing the processes it was required for. We discussed this during the Q&A portion of their presentation. This group also referenced but did not include examples from their phylogenetic analysis, and they struggled to answer why they chose their particular mutant because they lacked an understanding of it’s evolutionary conservation. In response to this omission by several groups I am expanding that activity for the re-implementation of these labs in Spring 2020.

Figure 2: This group did stated their hypothesis well and effectively used images from PyMol to justify their predictions. They proposed making a minimal mutation by changing the small nonpolar proline 119 to a small nonpolar alanine and making a separate maximal mutation by mutating it to the large nonpolar tryptophan. They predicted that the large amino acid would disrupt the enzyme’s active site (visualized by the presence of the yellow substrate). They showed that the tryptophan (the white wire structure above) was likely to disrupt protein structure by using the interaction model. They pointed out the large red interaction spheres where PyMol predicts two structures are attempting to occupy the same point in space as evidence that the protein’s structure proximal to the active site would be modified by this mutation.

Figure 3: Students show their final data. Partially supporting their prediction they observed both their minimal and maximal mutants displayed noticeably different enzyme activities. Their measurements for their minimal mutation are variable but it is possible that this enzyme retained some activity. These results will need to be repeated in future semesters, but the students seemed to learn and grown as scientists as they developed, tested, and refined their hypothesis.