Biochemistry labs

Teaching and Instructional Development

I have developed my teaching interests, approaches, and philosophy throughout my
scientific career, in particular over my experiences as Director of Laboratory Instruction
(DLI) in the Biochemistry and Molecular Biology Department at the University of
Massachusetts Amherst. I truly believe the objectives of a laboratory course must reflect
the necessity of (1) training life sciences majors using the wide array of current
procedures used in academic and industrial settings; (2) exposing students to the
scientific method with respect to experimental design, implementation, and analysis in a
student-driven fashion; (3) teaching students how to communicate their knowledge in
written and oral forms; and (4) preparing students to be successful after graduating with a
life sciences degree. I believe laboratory course offerings must evolve to stay current in
methodology and instrumentation to best prepare our students.
A sampling of innovations and initiatives I have developed for the laboratory courses I
actively teach are highlighted below, and are intimately linked to my teaching
philosophy. Finally, I firmly believe the most important role of any educator is to act as a
mentor for students. I strive to fulfill this critical role by inspiring interest in the life
sciences with high standards and expectations for student performance.
Biochemistry 526 General Biochemistry Laboratory for Majors
Biochemistry 526 is a four credit laboratory course with a mandatory lecture component
that is required of all biochemistry majors. This course is designed to provide a
foundation experience for conducting experiments in a biochemistry laboratory.
Experiments/techniques include spectrophotometric quantitation of DNA and proteins,
yeast genomic DNA analysis by restriction digest and PCR, yeast transformation with
functional and genetic complementation analysis, plant gene expression analysis by RTPCR, molecular cloning and bacterial transformation/selection/screening, protein
expression and affinity purification, and kinetic analysis of enzymes and inhibitors.
Experiments are continually updated to reflect the evolution of techniques, methods,
equipment, and approaches that biochemists face in the 21st century. A key facet of this
revised laboratory curriculum allows for more student-based experimental design, as well
as to instruct students in higher-throughput approaches they will no doubt utilize in their
careers.
Biochemistry/Chemical Engineering 590A Biochemical Processing Laboratory
Biochemical Processing Laboratory is a four credit laboratory course open to
biochemistry and chemical engineering majors, with a target 50/50 representation from

each major. This course is designed to provide a student-driven, project-based advanced

laboratory experience at the interface of the life sciences and engineering. Standard
biochemical techniques (i.e., molecular cloning, transformation, protein expression,
product purification, and enzyme functionality) and chemical engineering practices (i.e.,
quantitative analysis, systems integration, bioreactor scale-up and operation, and process
design) are utilized by students. Laboratory groups of four have students from each
major to direct the integrated approach of this course. A large component of the course is
developing communication skills (e.g., report writing, presentations, etc.) amongst the
students. The expected outcomes are to better train students in emerging interdisciplinary
technology, to form a partnership with industry (including a guest lecturer and facility
tour), and to increase the recruitment and retention of biochemistry majors.
Recently, students successfully cloned, expressed, and purified human protein
phosphatase I (hPP1), an enzyme whose functionality represents a target for anti-cancer
and anti-HIV treatments. This enzyme is currently studied in the research laboratory of
Dr. Jeanne Hardy (Department of Chemistry). The students used molecular
biology/genetic engineering techniques (i.e., primer design, polymerase chain reaction,
and restriction digestion) to move the gene (cDNA) encoding hPP1 into a protein
expression plasmid (the widely-used pET system). The students designed strategies to
express the maximal amount of hPP1 attainable in a large bioreactor, then tested and
optimized conditions to recover the enzyme trapped inside the expression cells. Students
next employed four distinct purification methods (salt precipitation, dialysis, gel
filtration, and affinity chromatography) to maximize both hPP1 recovery and
purification. The students generated the first reported tagging of hPP1 that aids in
maximizing the solubility, purification, and identification of this important enzyme!
Biochemistry 421 Elementary Biochemistry Laboratory
Biochemistry 421 is a two credit laboratory course with a mandatory lecture component
that is offered to human nutrition, animal science, and food science majors. This course
is designed to provide an introductory experience to conducting experiments in a
biochemistry laboratory. Students learn a broad spectrum of modern techniques and their
underlying physical, chemical and biological principles. Experiments and techniques
include spectrophotometric quantitation of DNA and proteins, gel filtration and affinity
chromatography, protein purification analysis by SDS-PAGE, DNA isolation, PCR and
RT-PCR, bacterial transformation, ELISA for disease detection and epidemiology, and
enzyme kinetics and inhibition. A major focus of this course is to convey the relevance
of biochemical processes and methods to the fields of animal science, human nutrition,
and food science.