Q 2010 by The International Union of Biochemistry and Molecular Biology BIOCHEMISTRY AND MOLECULAR BIOLOGY EDUCATION

Vol. 38, No. 5, pp. 317–323, 2010

Laboratory Exercises

Bringing the Excitement and Motivation of Research to Students;

Using Inquiry and Research-Based Learning in a Year-Long
Biochemistry Laboratory
PART I–GUIDED INQUIRY–PURIFICATION AND CHARACTERIZATION OF A FUSION PROTEIN: HISTIDINE
TAG, MALATE DEHYDROGENASE, AND GREEN FLUORESCENT PROTEIN.

Received for publication, December 1, 2009, and in revised form, February 16, 2010

Kristopher Knutson, Jennifer Smith, Mark A. Wallert, and Joseph J. Provost‡

From the Department of Chemistry and the Biochemistry and Biotechnology Program, Minnesota State
University Moorhead, Minnesota, Minnesota 56563

A successful laboratory experience provides the foundation for student success, creating active partici-
pation in the learning process. Here, we describe a new approach that emphasizes research, inquiry and
problem solving in a year-long biochemistry experience. The first semester centers on the purification,
characterization, and analysis of a novel fusion protein within a guided research experience. Throughout
the semester, students gradually acquire skills as they are allowed to work independently. A fusion pro-
tein, malate dehydrogenase-green fluorescent protein with a histidine affinity tag (MGH), is used
throughout the semester. The fusion protein allows for a high throughput analysis and is stable for dura-
tion of the semester. Students start with the purification and analysis of the plasmid DNA and end with
an enzymatic analysis of MGH. As students take ownership of their experiments and choose two differ-
ent chromatographic resins, they make many choices throughout the semester. Skills, motivation, confi-
dence levels, and attitudes were assessed before and after the semester. Students achieved high levels
of critical biochemical laboratory skills and critical thinking while increasing their confidence and motiva-
tion for working in a biochemical research setting.
Keywords: biochemistry laboratory guided, inquiry laboratory, malate dehydrogenase, green fluorescent
protein.

INTRODUCTION based learning (using ill-defined questions or experi-

Pedagogical Approach
The ability to think critically and independently in both
the design and execution of an experiment is crucial for
scientists. The best way to acquire this ability is through
hands-on research. The National Science Education
Standards describes inquiry as the ‘‘. . . process by which
scientists and students pose questions about the natural
works and investigate phenomena.’’ Further, ‘‘for stu-
dents to develop the abilities that characterize science
as inquiry, they must actively participate in scientific
investigations’’ [1]. Engaging students in a research-rich
environment will increase the crucial cognitive skills im-
portant for young scientists’ development. Providing an
enhanced experience for students is therefore critical to
increase both motivation and understanding [2–4]. Class-
room-situated Problem-Based Learning Curricula [5, 6]
and Process Guided Methods [6] provide effective meth-
ods of knowledge acquisition. In the laboratory, inquiry-
‡ To whom correspondence should be addressed: Tel: (218)
477-5085; Fax: (218) 477-2018. E-mail: provost@mnstate.edu.
This paper is available on line at http://www.bambed.org
ments where limited information is given to the student)
has enhanced student learning [7]. An in depth,
research-focused experience (where the outcome is not
clear and students investigate as active participants) is
often called research-based learning or project-based
learning [7]. What differentiates the two approaches is
the laboratory’s outcome: problem-based laboratory
instruction is predetermined with a student-derived
deductive approach [8], whereas the outcome for
research-based projects should not be known in advance
and should vary from year to year [7].
Typically the laboratories that accompany science
courses guide their budding scientists through a series of
unconnected experiments to demonstrate key principles
or techniques; these are often labeled ‘‘expository’’ or
‘‘skill-building style’’ laboratories [7, 8]. The outcome of
traditional laboratories results in students with good indi-
vidual skills but less higher-level understanding of the
research process [7, 9, 10]. In such a teaching lab, one
week students may be working on the kinetics of an
enzyme and the next week must focus on an unrelated
task, such as a DNA or lipid experiment having little or
no connection with previous or future labs. Unfortunately,
317 DOI 10.1002/bmb.20400
318
this training does little to teach students to become inde-
pendent in experimental design, execution, or analysis.
The result is new graduates that lack the ability to plan
or design experiments on their own [3, 7, 10]. Traditional
cookbook laboratories poorly serve the student learning
process because their step-by-step instructions help cre-
ate students who do not think about what the experiment
is or why they are doing it. Additionally, this style does
not enhance student understanding of the scientific pro-
cess. The statement, ‘‘I did everything in the instructions
but it did not work,’’ can often be overheard in laborato-
ries that use this method. In comparison, development of
both technical skills and a real understanding of the
‘‘process of science’’ are evident with inquiry and
research-based learning [10–14].
Research as a learning modality is highly valued for its
ability to teach students integrative and critical thinking
[2, 3]. Unfortunately, the opportunity for independent
research conducted by undergraduates is limited for
many reasons. A Science Policy Forum [15] discussed
and urged the implementation of an AAAS report on
reforming science education that asserted active and co-
operative learning is most effective. The 2004 Science ar-
ticle called scientists to involve students in research and
challenged more faculty to bring research to the class-
room and the students. More recently, another Science
article highlighted two programs that have been highly
effective in doing just that [16]. The evidence is impres-
sive for long-term retention of learning and motivation for
science among students who engage in research. In a
Howard Hughes Medical Institute-funded survey, stu-
dents who participated in a research project reported an
increase in their ability and motivation to work though
scientific problems and techniques and, 9 months after
their experience, over 87% of the students planned a ca-
reer in science [17]. However, there still remains a need
to engage a much larger number of students and one
way to provide this engagement is to incorporate a
research experience in their coursework. This project
gives students access to a research-focused experience
that is both meaningful and inspirational.
Description of Year-Long Project
This project is a two-semester biochemistry laboratory
based on both inquiry and research-based learning ped-
agogies. The first semester of the sequence is based on
the purification and characterization of a fusion protein
(watermelon malate dehydrogenase-green fluorescent
protein with a 6X His tag [MGH]). The first semester labo-
ratory can be a stand-alone set of experiments or can be
used to transition into a more research-based, follow-up
semester. The second semester laboratory (see part II)
builds on skills learned in the first semester, where stu-
dents are given a list of wild-type and mutant His-tagged
malate dehydrogenase (MDH) constructs, guided through
a series of bioinformatics and structural biochemistry
workshops and then asked to generate a testable hypoth-
esis using MDH. The remainder of the semester student
groups design and work on their research project. Both
BAMBED, Vol. 38, No. 5, pp. 317–323, 2010
semesters are designed to move the responsibilities for
planning and designing the work from the instructor to the
students in an open-ended research setting. Student
learning is supported by a number of general protocols
and web-based streaming videos. This approach allows
the faculty member to be more of a mentor than instructor.
LABORATORY DESIGN
Course Description and General Outline (Semester
One–Purification and Characterization of MGH)
The first semester laboratory (described here) can be
conducted with a single instructor and a class size of up
to 20–24. The course meets once a week for 3 hours.
Students work in groups of 2–3 throughout the semester.
Some of the work is independent (such as the beginning
tutorials and final paper); however, most of the work
throughout the semester is cooperative. As is typical for
upper-division science courses, this laboratory requires
some independent, out-of-class work; however, if
needed, most of the outside work can be held to a mini-
mum (one hour about three times for the semester)
based on each institution’s space and time limits.
Because our students typically carry 16–18 credit hours
and most have part-time employment, independent labo-
ratory days are built into each semester, 2 to 4 weeks
where there are no orientation lectures or prelaboratory
work. In these sessions, instructors open the laboratory
and allow students to work as independent research
groups. (Institutions with large multisection laboratories
can easily open their laboratories, and allow student
groups to work in reserved time slots as needed.) Conse-
quently, the instructor must learn to act more as a princi-
ple investigator or mentor than a traditional instructor.
The first-semester laboratory consists of a semester-
long project working with MGH. This fusion protein allows
students to work with a protein introduced in their lecture
(MDH) as well as utilize an affinity tag (6X His tag) and the
stable nature of MDH and GFP to create a project ame-
nable to a long term project without losing significant en-
zymatic activity or fluorescence. The GFP portion of the
chimeric protein allows for a high throughput in the pro-
tein analysis where the protein’s fluorescence is used to
detect the protein in various samples. High throughput of
fraction assay (both GFP and protein analysis) is accom-
plished with a plate reader (at the expense of a more thor-
ough protein determination analysis). The MDH’s enzy-
matic activity is retained in the fusion protein and is stable
enough to be analyzed at the end of the semester. The
MGH construct was prepared specifically for this labora-
tory by the authors and is available upon request.
Students will practice critical biochemistry skills
throughout the semester. Specific techniques and theo-
ries are woven into the project rather than being the
focus of a week’s activities. The semester starts with an
introduction to the project and a simple set of laboratory
math and pipetting exercises, moves to a DNA purifica-
tion and transformation of MGH, and then spends 4–5
weeks with students selecting two of six purification
techniques. This component of the course is followed by
a western blot and kinetic analysis of MDH. The bulk of

the student’s grade is based on a Journal of Biological
Chemistry-style manuscript written in sections throughout
the semester.
The laboratory’s goal is to ease students into self-reli-
ance and confidence in the scientific process. It will pre-
pare them for future work as they gain both the confi-
dence and scientific skills needed to troubleshoot prob-
lems and develop protocols. Specifically, students will
gain skills, such as pipetting, preparation of buffers and
solution, DNA manipulation, chromatography, protein
handling, SDS-PAGE and western blotting, enzyme
kinetics, and scientific writing.
Support
Protocols, handouts, resources and tutorials are all
placed on the web for student access at: www.mnsta-
te.edu/provost/BiochemistryLabI.html. In keeping with the
research orientation, resources for students combine
textbook style information and general protocols. Specific
instructions and guidance are given only occasionally as
experimental protocols. When appropriate, prelab quizzes
are also linked. Links, manuals, and protocols are found
at the bottom of the web page to give additional back-
ground and help for students to work at their own pace.
On-line streaming videos (Tegrity, Panopto, or other com-
mercial sources) are provided to train students how to
perform critical steps and complicated theory, as well as
how to use equipment or techniques (using a pH meter,
pouring gels, setting up chromatography equipment).
These video files are used in and out of the teaching lab-
oratory to assist the student groups as they progress
throughout the semester. An on-demand video stream
also allows for groups to work at different paces and
gives the instructor time to act as a mentor instead of
stopping the class to demonstrate a piece of equipment.
While our example uses a commercial system for video
streaming, any number of programs, including YouTube
video, would work well. The key is not in an expensive
suite of software and camera, but in tailoring this type of
video support for individual institutions and students. Two
textbooks are used both semesters as references for lab-
oratory work, protocols and writing assignments [18, 19].
Weeks 1-2 (Introduction and initial Training)
Before the project begins, an introduction is presented
to the goals of the semester, instructor’s expectations,
safety, and laboratory notebook requirements. Students
are organized into groups of 2-3 and told they are part of
a semester-long research project where they will receive
a plasmid containing the clone for a novel protein called
MGH. They are asked to isolate the plasmid, and trans-
form the clone into an appropriate strain of bacteria.
Next, students are told that, as the semester progresses,
they will conduct an on-line purification tutorial: they will
choose two chromatographic methods of a possible six
resins, prepare buffers, pour columns, analyze fractions
and prepare the protein sample for the next chromatog-
raphy. The semester finishes when each student analyzes
319
his or her samples by SDS-PAGE, western blot, and ki-
netic analysis. To allow students from different levels of
laboratory experiences to acquire important initial skills,
two standard laboratories–a traditional pipetting experi-
ment using bromophenol blue and a homework assign-
ment using laboratory math–start off the semester. The
pipetting experiment introduces the students to use of
the spectrophotometer, statistics, and graphing. An
unknown concentration of bromphenol blue can be
added into the experiment if an instructor wishes to use
this opportunity to introduce the use of standard curves,
as the concept of standard curves is used several times
throughout the rest of the semester.
Weeks 3-4 (DNA Purification and Transformation)
Students are given a plate or slant of LB Agar with E.
coli containing the MGH plasmid. In the introduction to
the semester, students were told that it is common to
receive a clone from a collaborator with the construct
transformed in a strain of bacteria appropriate for prepar-
ing DNA but not for protein expression. Therefore, the
student’s first job is to purify the plasmid DNA using a
commercial kit, quantify the purification and then to
transform an appropriate strain (typically BL21) of E. coli
for expression of MGH. The specific instructions use the
protocol from the commercial kit, which allows the stu-
dents to see the kind of support they would experience if
working in a research or industrial laboratory setting. Any
plasmid commercially available mini-prep kit would be
appropriate; we found that a spin column format made
for a more efficient use of time. Students are asked to
determine quality and concentration of the plasmid by
spectrophotometric analysis before finishing the first day.
Students will perform an agarose gel electrophoresis on
the following week. To speed the plasmid purification
along, a growing culture can be started in advance of the
lab and used for several sections. During week four, stu-
dents must transform competent cells (either commer-
cially obtained or prepared by the instructor). Cells are
plated in various volumes of cells without and with antibi-
otic and transformation efficiencies calculated (see class
webpage for specific handout). Students are instructed
that a positive colony will be selected for expression and
that a lysate bacterial culture will be prepared for them.
Lysate can easily be prepared well in advance; it is more
efficient to prepare several liters of induced culture and
freeze lysate into 15 ml aliquots to give to student groups
than to take time in the middle of the semester.
Week 5 (Writing Scientifically)
A significant goal of the semester is to improve the
students’ writing skills. Each student is required to main-
tain a laboratory notebook and to write a full manuscript
on the semester’s collective work. To support student
learning, an entire block of time is devoted to discussing
the methods and requirements of scientific writing. Par-
ticular attention is paid to each section of a paper as
well as to stfigure legends, graphing, presentation of
320
data, and formatting. We use the style guidelines from
the Journal of Biological Chemistry and provide specific
instructions for each section of the paper (see website).
Each student receives a full and detailed rubric for grad-
ing. Consistent feedback to the students throughout the
semester eases their writing process, and helps direct
those who have little scientific writing experience. Thus,
we find it is best to require sections and examples of the
paper to be written and turned in for review throughout
the semester. However, we limit the initial writing to par-
tial sections: e.g., we assign a graph and figure legend
from one of the first experiments, a method for the sec-
ond experiment and a results section for another experi-
ment. Requiring homework in this fashion provides stu-
dents with writing practice in bite-sized pieces and gives
a good opportunity for the instructor to provide them
with prompt feedback.
Weeks 6–11 (Protein Purification)
The following 6 weeks is the time for students to pre-
pare and purify MGH from 15 ml of MGH containing cell
lysate. To start this block, an on-line tutorial on chroma-
tography (see class website) and worksheet introduce
students to the key concepts of column purification
including: resin-preparation, appropriate buffers, and
conditions for protein binding and elution. In addition to
the web-based tutorial, students are given a purification
handout, which sets out student expectations for the
next 6 weeks, more information about MGH, and the
basics of chromatography (including how to design, pre-
pare chromatographies, load and run the steps, as well
as how to analyze and pool fractions). This document
also includes a series of key pieces of information vital
for the planning and progress of the work. Students are
required to choose two different chromatographic resins
from a list of six or more possible resins, use a purifica-
tion check sheet, and work with the instructor to approve
their proposed experimental plans. If needed, the stu-
dents could limit the experiment to a single purification
step. However, the logistics and challenges of preparing
samples for a second column would not be experienced.
Also, including more than one chromatography can
decrease the ability of copying results between groups if
the instructor ensures that groups do not use the same
series of chromatographic steps. Each student checks
out a set of equipment and two tubes of chromato-
graphic resin to use for the purification process. Frac-
tions will be analyzed for MGH by fluorescence and pro-
tein assay. The format for either assay will depend on
equipment and budget for each institution. A combina-
tion UV/Vis–fluorescence plate reader allows for a quanti-
tative high-throughput of student work; however, other
budget-minded methods (UV gel reader, or even semi-
quantitative analysis by students–high fraction is a rela-
tive fluorescence value of 10 and water is 0) have also
worked well.
Students are expected to conduct their purification
work as independent research groups for the next 4–5
weeks. If carefully monitored, most of the work can be
BAMBED, Vol. 38, No. 5, pp. 317–323, 2010
done in the 3-hour block. Depending on the institution,
students can work in or out of class time. Large univer-
sities with multiple sections could open the teaching labs
to students throughout the day. In this way, the lab is
open for 6 to 9 hours, or more, and instructors or teach-
ing assistants then act as mentors for whoever is in the
laboratory. Common stock buffers and reagents are
stored in a central and convenient location, facilitating
students’ preparation of their own buffers for the purifica-
tion.
Using more than one chromatography step utilizing
standard resins creates diversity in projects between stu-
dents and semesters. If needed, an instructor can
change the order of chromatographies among groups to
alter the results from group to group. Students have
found value in learning to prepare their samples between
chromatographic steps. Therefore, ultrafiltration, dialysis,
ammonium sulfate precipitation, or pH adjustments are
possible manipulations that students must consider
before moving on to the next chromatography step.
Such choices result in another critical thinking opportu-
nity. Timing of experimental preparation and execution
during this phase becomes important as mistakes are
made and delays can happen. It is important for the in-
structor to stay on top of what the groups are doing and
make clear that work must be finished before the next
step (SDS-PAGE and western blot). If a research group
makes a mistake, students can receive another aliquot of
lysate and start over. Because we are more concerned
with learning than final product, points are not lost for
low yield or lost samples unless the mistake is repeated.
Weeks 12–13 (SDS-PAGE and Western Blot Analysis)
Because of time, budget, and equipment constraints,
we found it best if all students conduct the SDS-PAGE
and western blot analysis as a class at the same time.
Depending on the individual institution capabilities, stu-
dent research groups can cast and store their entire gel
the week before SDS-PAGE, or gels can be precast
(whole gels or just the resolving gels, or alternatively,
using the NEXT gel–a one piece gel system) by the in-
structor before the start of the laboratory. Depending on
budget and equipment availability, a group can use one
gel divided into halves: one half used for Coomasie stain-
ing and the other half to be transblotted. Because of tim-
ing, this lab needs a more traditional approach. Thus,
students receive a more straightforward experimental
protocol. Either the instructor or students can retrieve the
blots and place them into a blocking buffer for storage in
a closed container at 48C until the following laboratory
session. Western blotting can be conducted using any
detection method. We found that a colorimetric HRP-
linked secondary antibody worked very well. Anti-GFP or
anti-His primary antibodies (commercial or generated in-
house as an independent research project) gives strong
results with the amount of MGH loaded onto most gels.
Increasing the concentration of the primary and second-
ary allows for a shorter incubation time (30 minutes at
room temp) to fit the time constraints of a three-hour lab-

oratory. Simple hand-rocking will work during the anti-
body incubations. A simple digital camera works well to
capture both the gel and the final blot. During downtime,
students can be introduced to the kinetic analysis basics
they will conduct the following week.
Weeks 14-15 (enzyme kinetic analysis)
During this block, students learn the basics of the en-
zymatic assay. If needed, unused lysate or commercial
MDH can be used if students have lost activity in their
sample or these can serve as positive controls while stu-
dents learn the basics of conducting real-time assays.
Students receive a basic protocol and are asked to
design their own experiments to determine Km and
Vmax for the assay. For those laboratories that meet
more than once a week, a much deeper kinetic analysis
can be conducted using an inquiry format [20, 21]. Week
14 is typically spent working with groups as they design
their procedure, while week 15 is devoted to conducting
the experiment and graphing the results. If time permits,
this data will be included in the final paper; however, as
drafts should have already been turned in for review,
including the kinetic data may be a challenge.
GRADING
To ensure that the process and critical thinking, rather
than yield or ‘‘correct results,’’ are the focus of the se-
mester, half of a student’s grade depends on the final pa-
per. By completing a JBC style manuscript, students are
forced to think critically about the experiments com-
pleted throughout the semester and evaluate their re-
spective results. To ensure that students are rewarded
for appropriate attention for benchwork, a small fraction
of points (20%) is assigned to various results determined
from the laboratory notebook and the paper. Drafts of
the various sections of the paper also receive points,
while the notebook receives 15% of the grade.
EQUIPMENT
The semester’s experiments were designed to accom-
modate a typical upper-level chemistry/biology labora-
tory. As discussed earlier, a UV/Vis, fluorescence plate
reader is helpful for processing a large number of stu-
dents and providing quantitive analysis of their protein
assays and MGH fluorescence assays. However, as
described above, other means of determining each frac-
tion’s fluorescence can be implemented to meet equip-
ment limitations. Resins are a significant cost for a labo-
ratory. Typically, 2 – 5 ml of most resins is sufficient (with
the exception of SEC columns, which require a column
volume of 50 to 80 ml). These resins are easily reusable
and if needed, one could start with 2 or 3 resins and add
a different resin each following year. Nickel-Agarose res-
ins are often used once or twice by biotechnology or
pharmaceutical companies and then thrown away. A sim-
ple survey of several such companies found that they
could donate used resins to an academic department. To
stretch a budget, a thrifty instructor can easily use and
reuse, for instance, ultra filtration and centricon items for
321
several semesters. Larger budget items include glass
columns, column adaptors, fraction collectors, and peri-
staltic pumps. Each group receives one column and
adaptor and is instructed to pour its own column. Inex-
pensive and simple peristaltic pumps are found in several
scientific catalogs for about $200. Some of the experi-
ments do not require fraction collectors or pumps and
therefore purchasing a handful of fraction collectors and
pumps can support double the class size. Reagent costs
are minimal as most of the buffers and other reagents
are common and inexpensive. Thus, a department with a
limited budget could ease its way into such a lab by
adding one or two pieces a year.
ASSESSMENT
This laboratory was conducted for three years with a
total of 68 students resulting in a 91% retention rate.
Formative assessment was conducted throughout the
three years to assess student learning, resource quality,
and the semester’s design. Each year of the evaluation
period, all students received a skills assessment tool
before the semester, at the end of the semester, and at
the end of the following semester. This skills assessment
focused on key concepts and biochemical techniques.
Its topics include working with buffers, dilutions, and pH
problems, quantization of DNA and protein, chromatogra-
phy, purification steps and protein analysis. Two different
faculty members graded the tests. The average pretest
scores were less than 20% while the post-test assess-
ment averaged 88%, with scores ranging from 74 to
98%. The follow-up skills from one year-post course
assessment scored 85%, indicating a high retention of
basic laboratory skills.
Additional formal assessment of student motivation
and attitude to research based learning and their own
skills appears in Table 1. All questions concerning the
student’s appreciation for noncookbook, open-ended,
research style learning showed an improved 0.33–0.53
step. As students were neutral to slightly against stand-
ard labs before the experience, the assessment shows
increased affinity for this style of teaching. Key points
included:
• Student opinion on research style labs was ‘‘neutral-
agree’’ (3.4) before the semester but shifted to
‘‘agree to strongly agree’’ (4.19) after the semester.
• Students greatly increased their confidence in their
understanding of biochemistry. This item correlated
with their post-test skills test.
• Students’ confidence in their critical thinking, writing
and communication skills increased from 0.5 to 0.25.
• The classes showed a 91% retention rate (68 stu-
dents started over 3 years, 62 finished).
• Most students enjoyed the experience and found
they had better skills. Some students were chal-
lenged by the open-ended nature of the laboratory.
DISCUSSION
This semester’s goal was to provide an opportunity for
students to engage in an inquiry-style learning experi-
322 BAMBED, Vol. 38, No. 5, pp. 317–323, 2010
TABLE I
Biochemistry Laboratory I - Pre & Post Assessment - Numbers in parenthesis indicate the average response in the
pretest/post test assessment
Strongly Strongly Not Do not
disagree Disagree Neutral Agree agree applicable know
1 I often didn’t understand the 1 2 3 4 5 6 7
concept behind the lab
experiment (2.62/2.09)
2 I like labs where I get to help 1 2 3 4 5 6 7
design an experiment to
answer a question (3.69/3.8)
3 I prefer a course where there are 1 2 3 4 5 6 7
provided opportunities for me
to help design experiments
(3.70/4.04)
4 I prefer doing labs that are more 1 2 3 4 5 6 7
like following a recipe in a
cookbook (3.11/2.71)
Assuming that all the following activities are equally well-implemented, I learn well by . . .
5 Doing homework assignments 1 2 3 4 5 6 7
(3.50/4.22)
6 Using computer based material 1 2 3 4 5 6 7
(3.57/3.62)
7 Listening to lectures (3.51/4.23) 1 2 3 4 5 6 7
8 Reading a textbook (3.42/3.67) 1 2 3 4 5 6 7
9 Doing fill in the blank style 1 2 3 4 5 6 7
laboratories (3.19/3.04)
10 Conducting research-style 1 2 3 4 5 6 7
laboratories (3.45/4.19)

For the following questions, rate your understanding of and attitude in science in the following areas:
Not at all Just a little Somewhat A lot A great deal Not applicable Do not Know
11 Understanding main concepts of 1 2 3 4 5 6 7
science and biochemistry or
biotechnology (2.94/3.78)
12 Ability to think through a 1 2 3 4 5 6 7
scientific problem or argument
(3.57/3.85)
13 Critically reviewing scientific 1 2 3 4 5 6 7
papers/literature (2.90/3.39)
14 Critically thinking about what 1 2 3 4 5 6 7
your are doing while at the
bench (3.45/3/71)

Answer the following questions in terms of the important aspects of your scientific career.
Not at all Just a little Somewhat A lot A great deal Not applicable Do not know
15 Confidence in my ability to learn 1 2 3 4 5 6 7
new and difficult things (3.97/
4.24)
16 Problem solving skills (3.94/4.19) 1 2 3 4 5 6 7
17 Lab techniques (3.71/4.07) 1 2 3 4 5 6 7
Think of the goals you had for yourself going into this course. Did you meet or exceed these goals? How did the laboratory style and
make up help or hinder your expectations.

ence where they became more independent in planning
and conducting their work. Specifically, the semester
aimed to improve students’ learning abilities, to enhance
their motivation as scientists, and to improve their confi-
dence as student researchers. While this style of labora-
tory works well with motivated students, even those stu-
dents who are shy or more accustomed to working in a
traditional setting felt they gained from the experience.
However, faculty wishing to adapt such a program will
need to take an open-minded approach to changing the
way an instructor interacts with class. The instructor
must be more of a resource or mentor than supervisor.
Use of the streaming videos and on-line tutorials and
protocols is not intended to tell the students step-by-
step what to do. Instead, they simulate the type of proto-
cols and resources typically found in a research labora-
tory. As such, the laboratory manual and handouts are
guides.
The process is more important than the product. As
one observer asked, ‘‘How many would be willing to give
$40 to 50 thousand to a bunch of students to go to
Home Depot, buy the materials to build a house and rea-
sonably expect to be able to see a home built and habit-
able in a couple of months with no prior training?’’ The
answer is: we are not doing this to build a house but to
create a gifted and motivated set of carpenters. Assess-
ment of this data shows that we are achieving this goal.
A hands-on, research-rich experience can be well pro-
vided for a wide audience within this two-semester labo-
ratory procedure.

Acknowledgment— The authors would like to thank Dr. Ellis
Bell for his support and encouragement as well as to Dr. James
T. Hazzard, Department of Biochemistry and Molecular Biophy-
sics at the University of Arizona, for his critical eye: appreciate
his insight and candor about this learning style. The authors
also like to thank one of the students, Anusha Mishra, for ask-
ing, ‘‘Why not make a MDH-GFP-His tagged clone’’? Your wild
idea worked out pretty well.
This work was supported by the National Science Foundation
through grant number CCLI DUE 0511629 and by the Minne-
sota State Colleges and University Center for Teaching and
Learning.
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