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Keywords:

  • biochemistry laboratory;
  • research-based learning;
  • malate dehydrogenase

Abstract

  1. Top of page
  2. Abstract
  3. INTRODUCTION
  4. LABORATORY DESIGN
  5. GRADING
  6. ASSESSMENT
  7. DISCUSSION
  8. Acknowledgements
  9. REFERENCES
  10. Supporting Information

Research-based learning in a teaching environment is an effective way to help bring the excitement and experience of independent bench research to a large number of students. The program described here is the second of a two-semester biochemistry laboratory series. Here, students are empowered to design, execute and analyze their own experiments for the entire semester. This style of laboratory replaces a variety of shorter labs in favor of an in depth research-based learning experience. The concept is to allow students to function in independent research groups. The research projects are focused on a series of wild-type and mutant clones of malate dehydrogenase. A common research theme for the laboratory helps instructors administer the course and is key to delivering a research opportunity to a large number of students. The outcome of this research-based learning laboratory results in students who are much more confident and skilled in critical areas in biochemistry and molecular biology. Students with research experience have significantly higher confidence and motivation than those students without a previous research experience. We have also found that all students performed better in advanced courses and in the workplace.


INTRODUCTION

  1. Top of page
  2. Abstract
  3. INTRODUCTION
  4. LABORATORY DESIGN
  5. GRADING
  6. ASSESSMENT
  7. DISCUSSION
  8. Acknowledgements
  9. REFERENCES
  10. Supporting Information

This project is the second semester of a year-long research experience for undergraduate biochemistry students. In the first semester [1], students were steeped in a research-like environment, where they planned and conducted guided inquiry experiments. In the project described here, students work alone or in small groups throughout the semester on an independent research project centered on a series of wild-type and mutant affinity-tagged malate dehydrogenase (MDH) clones. This is a required course for biochemistry and biotechnology majors and the class meets one day each week for 3 hours. Students are expected to work on their project 1 to 2 hours a week outside class time to complete their projects. This type of laboratory experience has worked for class sizes up to 30 students and typically is performed with a single faculty instructor without teaching assistants.

Research-based learning is similar to the studio format: in both teaching and laboratory classrooms, they enhance learning by allowing students to behave like scientists [2]. Inquiry laboratories differ from research-based learning in that they place more responsibility on students to look at the big picture, design experiments in a hypothesis-driven fashion, and to increase their intellectual autonomy [3–5]. Some of the early innovators of the studio format began at Rensselaer Polytechnic Institute, where a year-long lecture and laboratory was used effectively to teach molecular biochemistry metabolism [6]. In a similar fashion, faculty at Kansas State University have redesigned their entry-level biology course into a semester-long research problem. Assessment of the Kansas State project outcomes showed that students found this an exciting learning method for students with many different learning styles. A semester-long research format also works for upper-level science students [7–9]. David Rivers at Loyola College in Maryland incorporated an inquiry-based laboratory for an upper level physiology course that elevated student excitement and a commitment to learning [8]. Research-driven learning has also been successfully adapted for an advanced microbiology course, which increased the research productivity of many of the undergraduates and their readiness to perform meaningful research after they left the teaching laboratory [9].

This year-long project resulted from the assessment of our senior students in the biochemistry and biotechnology major. Our assessment showed that students without research experience were much more timid in the laboratory and were much less prepared to conduct independent research than their research-experienced peers. Therefore, we began to incorporate inquiry- and research-based learning into several of our teaching laboratories. The two-semester biochemistry laboratory sequence presented here is primarily a junior-year course, the natural point in time to enhance the research experience for our students. One of this project's specific goals was to decrease the gap in confidence and ability between students with and without research experience. Our goal was also to raise the motivation of students for science. Additional goals for the research setting were: to increase students' ability to read primary literature critically, design independent and novel research, and use structural and bioinformatics databases in making their hypothesis.

The research-based learning described here uses the growth of student learning and confidence gained in the first semester as a springboard to fully release the students into a research-based environment. This was created in a manner similar to that conducted by J. Ellis Bell at the University of Richmond [10]. While either semester can work as a stand-alone teaching laboratory, the combination of the two laboratory experiences enhances the abilities of students with a laboratory experience, gives confidence and acumen to those students without a prior research experience and effectively increases student motivation and learning. Supporting assessment and learning resources are posted online.

LABORATORY DESIGN

  1. Top of page
  2. Abstract
  3. INTRODUCTION
  4. LABORATORY DESIGN
  5. GRADING
  6. ASSESSMENT
  7. DISCUSSION
  8. Acknowledgements
  9. REFERENCES
  10. Supporting Information

Course Description and General Outline (Semester Two–Malate Dehydrogenase Centered Research)

This semester's goal is to fully immerse the student into a research environment that builds on the foundations created during the first semester of biochemistry laboratory (Knutson, 2009). Students first work through a short series of tutorials on bioinformatics and protein structure, they conduct a literature review of MDH and then, using an existing list of MDH clones and mutants from a variety of sources, they derive a hypothesis to test for the rest of the semester (www.mnstate.edu/provost/BiochemlabII.html). The students can choose the type and scope of experiments with guidance from the instructor. In keeping with research-based learning, it is critical that the mentor/instructor guide the students to create original research projects and avoid preset activities that have been conducted several times in the past. This means that the instructor must take on the same role as a principle investigator [3, 4]. Faculty mentors should actively guide the laboratory students into worthy and novel projects. The nature of the work suggested and performed by these students has ranged from standard kinetic analysis of MDH mutants to microwave-assisted proteolysis and reverse phase chromatography of the resulting digests. Over the past few years, we have created a range of different wild-type and mutant His-tagged MDH constructs (see website for list), which are available to continue the research based projects. Thus, this semester intends to allow the instructor to become a principle investigator and the student a bench researcher. Here, instructors are responsible for mentoring students through their projects, providing planning advice, offering insight as students execute their experiments, and assisting students as they interpret the results of their work. At the end of the semester, student present their work as a research seminar. Each group is responsible to find and create its own protocols, experimental design, and to interpret its own data.

A number of universities incorporate research into their classroom. These experiences are often a part of an instructor's funded research or organized so that each research group has a different project. Either way, while an effective teaching tool, these models can nevertheless be a challenge in three areas: to apply year to year, to adapt for larger institutions with several lab sections, and to adapt for faculty at small schools with a limited budget. We propose that research using a common protein (MDH) can bring a reasonable model of in-depth research-based learning to a larger audience. Keeping the research projects to a common enzyme is critical for a number of reasons. Faculty and teaching assistants need only to learn one enzyme; a shared theme for the semester does not require an instructor to be an expert on many subjects. Instructors only have to provide a set of stock reagents for the class projects, minimizing the time needed to prepare laboratory regents throughout the semester. This decreased preparation time allows the instructor to focus on mentoring the students. Students gain from the shared experience because the common protein encourages cooperation and mutual leadership among groups. Using MDH also brings economy to laboratory costs. The enzyme assay is inexpensive and the kinds of experiments students can perform can easily be tailored to the available equipment and faculty background.

The class website provides a series of handouts to the students to guide them through the process. As students are required to work on the projects at their own pace, they have only a few required class attendance dates. If an institution allows, students can come and go to work at their own pace on their own research projects. If limited space prevents this option, most of the work can be done within a 3 to 4-hour a week laboratory. For larger universities with multiple sections, this type of laboratory could easily be done in laboratories opened for several hours each day. Students could sign up for a time and work with the teaching assistant or faculty instructor. While very different from the standard approach to a class, this arrangement could offer teaching assistants the opportunity to become mentors and better laboratory leaders. We have also found that a series of deadlines for specified project goals and objectives, giving them assigned point values, helps keep the students on pace.

Phase I (Bioinformatics, Structural Biochemistry and MDH Background)

This phase focuses on a self- paced exploration of bioinformatics and modeling databases using tutorials and handouts provided by the instructor. Students are also asked to conduct a thorough literature background of the catalysis, regulation and the biochemistry of MDH. To support their work, students are provided handouts and several 10-15 minute videos on searching, aligning nucleotide sequences, and working with amino acid and protein structure databases. The goal is not to become a bioinformatics course or to make the students experts in using a specific program, but to give enough experience to allow the students to conduct research on their protein. The flash files (SWF) are audio and video captures of a computer screen as an instructor walks students through each of the tutorials on using the database and modeling programs. Students receive a companion handout, “Informatics and Modeling Workshop,” with a specific set of instructions using phospholipase D as an example protein. Freeware is used to reduce the cost and avoid an investment in expensive programs larger than the scope of an undergraduate laboratory. We have found that once students are exposed to and understand the basics of using databases and rendering pdb files, they are much more interested and willing to invest the time to learn more complicated programs.

We have chosen to narrow the training on these databases and modeling to the tools and steps necessary for a good understanding of the research project students will be conducting. They first are asked to search Pub Med for nucleotide and amino acid sequences. Students then use the tutorials and handouts to learn how to align nucleotide and amino acid sequences. Specific attention is paid to the practical aspects of using a sequence to find coding DNA sequence numbers, domains, aligning sequences, and differences between nucleotide and amino acid records. These are particularly useful skills when students begin to compare the important domains and residues in an MDH found in a publication vs. the MDH clones students will be working with. Finally, students are required to complete a series of video demonstrations on the modeling software. Students use the videos to learn how to search the protein database and perform basic rendering steps. Then they are asked to overlay similar structures, zoom in on specific domains, change amino acids and highlight the changes in their rendering and then to create a high-quality final rendering of their protein. A homework assignment asks a series of specific questions that culminate in a solved structure of MDH.

A number of well-designed workshops and tutorials explain how to train students on these databases [11–13]. The specific program and method will depend on instructor expertise and university support. For our laboratories, we have used the freeware available on the National Center for Biotechnology Information (NCBI) for molecular databases and structure databases. Several good programs render and compare protein structures including Cn3D, VAST, Protein Explorer, and PDB Swiss View. We use pymol for most of our rendering work and, collaborating with another university, have created a YouTube channel. One challenge in teaching an introduction to these programs is their volatile nature. As their interfaces with the web and databases change, tutorials and handouts may well need to be updated each semester. We highly recommend that all instructors create their own tutorials tailored to meet their specific needs.

Students are then asked to search the literature to find information on the structural, kinetic and catalytic features of MDH. This assignment guides the students through an in-depth study of MDH. Students are asked to perform this work independently and not work as a group until after this work has finished. They are given 2-3 weeks to do this phase, although less time would certainly be appropriate.

Phase II (Hypothesis Development, Experimental Design, and Proposal Presentation)

Students then form into groups and work as a team to review a list of MDH clones (each 6X His tagged expressed in E. coli) provided as glycerol stocks to the students. Over the past several years, we have assembled and created a number of wild-type and mutated MDH isoforms for students to use in their projects. These clones include: The GFP-MDH fusion protein used in the first semester (MGH), Watermelon glyoxisomal MDH and over 20 mutant versions of the plant enzyme. A short list of these mutants include: a MDH to LDH conversion, active site mutations, temperature stable mutants, NADH-NADPH mutants, mobile loop substrate binding mutants and others. We have also prepared or were given several other isoforms of MDH for students to us. These include Rat Liver Mitochondria with three mutants, Yeast MDH with 6 mutants, Photobacterim with two mutants, wild-type MDH from Chloroflexus and a Trichomonas MDH wild-type and a LDH-like mutant. Because only a few of these mutants have been published, the potential for meaningful research is very high. In all cases, students are not simply to repeat a published experiment and instead must look at another approach. As we have found that a point mutant published for one species or isoforms may not function similarly in another species, students can easily find a relevant research project. The structures for the E. coli and Watermelon enzymes have been published and several good reviews on the structure and function of MDH isoforms of the enzyme are available to facilitate the student's work [14–17]. A complete list of wild-type and mutant MDH isoforms will be produced and made available for use at other institutions in the near future.

Students receive the accession number of each wild-type MDH and a list of the various mutations, but they do not receive information on the identity of the mutants' function (remember, the specific species has not been published). Using the instructor's guidance, a literature search, and the structural work conducted in phase I, students are expected to determine what these mutants might be and must create a hypothesis and a short research proposal with an appropriate experimental design. The students are allowed to create any MDH related project. With a large number of wild-types and mutants available, no group needs to work on the same project year-to-year. Students are encouraged to think creatively, to base their hypothesis on observations from the literature and a structural analysis of the protein, not speculation. Students are required to plan and execute all phases of their work, including expressing and purifying (if necessary) the recombinant protein(s), designing protocols, developing method, and determining appropriate controls. The types of projects could easily include a large number of classical kinetic investigations of the purified proteins. However, students often look beyond the obvious to work on projects with interesting twists and outcomes. A short list of recent projects include:

  • Large-scale purification using FPLC and generation of crystals for x-ray diffraction of MGH.

  • Protease / proteomic analysis of MDH isoforms and other purified enzymes using two different proteases.

  • Tryptophan fluorescence studies using isoforms of MDH and urea to measure folding stability.

  • In-Gel MDH assay - technique development.

  • Kinetic analysis of MGH and watermelon MDH.

  • Substrate specificity of mobile loop mutants.

  • LDH-like activity after site-directed mutagenesis.

  • MDH–Citrate Synthase protein-protein interactions using size exclusion chromatography.

  • Temperature stability between wild-type (two isoforms) and mutant MDH.

  • Preparation of highly purified MGH, GFP and MDH to generate antibodies for ELISA and immunoblots.

  • pH stability of wild-type and mutant MDH activity and folding.

  • Optimization of expression and inclusion body formation of MGH and MDH.

Student groups are given a week to come up with a hypothesis, the observations for their hypothesis, and a basic plan. Students then meet with the instructor during the laboratory to review and modify their plan. They consider how to frame their hypothesis, kinds of experiments that are reasonable and will test the hypothesis, and the appropriate controls to include for their work. Each student in the group must have at least one clone/protein to work with in the project. For example, if three students in a group generate a hypothesis stating that a MDH Asp–Ala or Asp–Lys mutation will decrease specificity for substrate, one student will be responsible for working with the wild-type MDH, another for the Asp-Ala MDH mutant and the third student will work with the Asp-Lys MDH mutant. All students will work together on their project planning, expression, purification, and assay, but each student will be responsible for a significant separate portion of the project. After meeting with the students, the instructor will then specify specific project expectations for the group and each student. As mentioned earlier, these expectations include a timeline with objectives. This timeline clearly defines what should be accomplished to earn the desired grade and helps to limit inflated expectations. Finally, each group creates a 5-minute presentation on its hypothesis, experimental aims, and approach.

Phase III (Execution of Research Proposal and Final Presentation)

During this phase, students are expected to work independently on their projects. For many students, this is their first independent research project and procrastination can be a significant obstacle. To help them avoid procrastination, it is important to provide feedback and deadlines for trigger points. Here is an opportunity for the instructor to act as a principle investigator, checking in on the progress of the research group, reviewing results and providing insight on future plans. Another challenge for students is how they interpret results. If the data do not look perfect or “textbook like” undergraduates will often consider such an outcome as a failure. Students often overlook other functions, such as repeating experiments and use of statistics, and they should be guided and encouraged to include these functions in their project. For both the students and the instructor, this is the most exciting part of the semester, where students begin to feel confident, as if they are indeed young scientists. Holding regularly scheduled but informal progress meetings with the groups is critical to assess the students' progress and guide them through the semester.

During finals, students present their work. The presentation must include a structural rendering of their protein or mutation, an introduction to the project, their hypothesis and how the hypothesis was generated. The presentations must also include the methods, results and conclusions of their work. Students are given 12-15 minutes to present their work to the course and given a peer evaluation.

GRADING

  1. Top of page
  2. Abstract
  3. INTRODUCTION
  4. LABORATORY DESIGN
  5. GRADING
  6. ASSESSMENT
  7. DISCUSSION
  8. Acknowledgements
  9. REFERENCES
  10. Supporting Information

The bulk of the student's grade will be on the process rather than on a final positive result. Equivalent points are given for the homework in the first phase, and lab presentation (100 points). The laboratory book is turned in four times for review throughout the semester for a total of 200 points. The research proposal presentation is assigned 50 points. The instructor is required to maintain a log of his or her observations of how students function in their meetings and during their experiments: an additional 100 points are assigned for laboratory/bench acumen, based on the instructor's observation. A rubric can be prepared to assign these points. Finally, each student is given an opportunity to provide 10 points of peer evaluation points.

ASSESSMENT

  1. Top of page
  2. Abstract
  3. INTRODUCTION
  4. LABORATORY DESIGN
  5. GRADING
  6. ASSESSMENT
  7. DISCUSSION
  8. Acknowledgements
  9. REFERENCES
  10. Supporting Information

This course is only required by biochemistry and biotechnology majors; however, of six nonmajor students registered for the course, two switched to the major after completing the course. Two-thirds of the students continued from the first semester. The course was taught for 3 years, with a total of 44 students enrolled in the course having a 95% retention rate. At the beginning and end of each semester an eight-question survey was given to each student to assess the interest, motivation, and confidence changes mediated by this course (see Table I).

Table I. Student Confidence and Motivation Assessment Survey
  1. Students were given the same set of questions before and just after completing the second semester of biochemistry laboratory. Individuals were asked to answer based on a seven-point numerical system, seven being the highest and one the lowest. Numbers in parenthesis indicate the average response in the pretest/post test assessment.

1How do you feel you were prepared to conduct independent laboratory work? In other words, how well did you feel you would do if you were in a job or research lab that required you to do biochemical type activities? (4.02/5.93)
2Do you feel you understand more about biochemistry than if you would have conducted a traditional type of laboratory (a traditional laboratory are fill in the blank single day experiments)? (4.39/5.80)
3How do you rate your ability to think through complex biochemical laboratory problems or through the scientific process? (4.24/6.20)
4Has a laboratory of this nature helped your motivation to become a scientist (reinforcing your beliefs should also be considered)? (5.20/6.07)
5How do you rate your ability to think through complex biochemical laboratory problems or through the scientific process? (4.41/6.05)
6If you have worked in a research lab skip this question–Do you feel this laboratory has HELPED you become more proficient to work in a research lab? (4.79/6.54)
7If you have NOT worked in a research lab skip this question–Do you feel this laboratory has HELPED you become more proficient in your work in a research lab? (5.27/6.55)
8In both the first and second semester laboratories, you have had to write several assignments (including the MGH paper) and present. Do you feel both of these laboratories have helped you to write more effectively, to communicate as a scientist and to better use the resources of a scientist? (4.74/6.20)

The students' motivation, interest and confidence were generally assessed as very high. Students increased their confidence in preparing to conduct independent research by two units. Another of the goals for this in depth research experience was to enhance student retention in science courses. These data show that students were more motivated to stay or become scientists by 0.88 evaluation units. In another important outcome for this project, the gap of confidence and motivation decreased between students with a prior research experience and those without a significant research history. The assessment showed that students without research experience started the semester with lower confidence in their abilities than those with research students by 0.8 evaluation units. However, by the end of the semester, both groups felt they had learned enough to function well in the laboratory, a 1.5 increase for non-research students and a 1.27 increase for research students. Both groups rated themselves with a 6.55 of 7.0 at the end of the semester. Additionally, we found that students who participated the whole year felt they increased from 4.75 to 6.2 of 7 on their ability to communicate as scientists.

Critical thinking skills were assessed using the interview log from the informal meetings and the student presentation. In both cases a standard rubric, based on the Field-tested Learning Assessment Guide Classroom Assessment Techniques Scoring Rubric [18], was used to define the competency. Critical thinking skill components assessed were:

  • the ability to identify a hypothesis based on literature and structural information

  • the design and completeness in the research proposal, aim and specific experimental plans

  • the student's ability to analyze, interpret and make judgments in the course of an experiment

  • laboratory acumen

  • student ownership and engagement

  • the integration of ideas into a coherent argument and solution in the work and presentation

  • communication of results and one's thinking

Critical thinking assessment was placed in three categories, Highly Competent, Competent, and Not Competent. Of the 44 students enrolled in three semesters, 4.5% of the students were rated not competent, 49.5 % were rated competent and 46% were rated highly competent. In most categories students exhibited good critical thinking skills and, with some initial guidance on how to think more scientifically, students were able to use existing observations to generate strong questions for testable hypotheses. As indicated by the self-assessment, students were highly engaged and motivated for independent research work. One area needing work is in the student's ability to interpret results. Often, students either looked for the quick answer or interpreted anything less than a perfect, textbook-like, result as a failure. While no control exists as a comparison, it was clear that students did increase their interest and confidence in science and were able to either maintain or gain a high level of competency.

This work can also be assessed by the number of regional presentations generated by students working on their projects. Students at local or regional science meetings presented eight poster or oral presentations on novel research from this second semester of the project. An additional, anecdotal, result is that the students who continued from this course into a research laboratory or the research-intensive capstone course at our university have become much more productive and excited about their work. Faculty advisors are genuinely aware of the impact of this type of teaching laboratory and have come to expect a higher level of preparedness from students going through this course.

DISCUSSION

  1. Top of page
  2. Abstract
  3. INTRODUCTION
  4. LABORATORY DESIGN
  5. GRADING
  6. ASSESSMENT
  7. DISCUSSION
  8. Acknowledgements
  9. REFERENCES
  10. Supporting Information

The work presented here can be used, and is effective, as a mechanism to bring a research experience to a large number of students. The laboratory described here can be used as a stand-alone experience for a single semester of biochemistry (with modifications) or as part of a two-semester experience. We have conducted many types of research-based learning for several years and have found a number of benefits. Using a single set of proteins for the focus, for instance, increases the communication between students and decreases the chaos of having multiple different research groups in a single laboratory with one instructor. The organization of this semester-long research-based laboratory will allow a larger institution to offer several sections of the same laboratory with multiple instructors. A well-defined but open-ended project, it offers an almost endless set of research project options for the students as the common set of tools and required resources reduce the expense needed to support the semester. We believe the students gain in both critical skills and confidence. Like those in the Lapatto study, our students gained confidence and maintained key skills with the effects of the research participation persisting over time [19]. More importantly, our initial hypothesis that a research-based laboratory would decrease the gap between sets of students with different experiences was clearly supported by their self-reported confidence levels (Table I). The work presented here supports the importance of research in a classroom setting as a means to provide critical thinking and learning skills traditionally provided to small groups in a pure research setting [5]. In a recent report by the American Society for Biochemistry and Molecular Biology (ASBMB) for the Teagle Foundation, undergraduate research was highly regarded and presented as a centrally important, indeed crucial, experience for the proper preparation of scientists [20]. It is important to note that the authors of this report asserted that “Research-like courses may be a good preparation for a real research experience, but they cannot serve as a substitute.” We agree that little can replace a one-on-one mentored research experience: laboratory pedagogy of this nature can fill gaps and provide an experience for a much broader audience. This project has had a significant impact on many students who might not otherwise have gotten a chance to gain an experience in a research laboratory and learn the joys of becoming a scientist.

Acknowledgements

  1. Top of page
  2. Abstract
  3. INTRODUCTION
  4. LABORATORY DESIGN
  5. GRADING
  6. ASSESSMENT
  7. DISCUSSION
  8. Acknowledgements
  9. REFERENCES
  10. Supporting Information

The authors would like to thank Dr. Ellis Bell for his support, insight and the initial MDH clone to make this project happen.

REFERENCES

  1. Top of page
  2. Abstract
  3. INTRODUCTION
  4. LABORATORY DESIGN
  5. GRADING
  6. ASSESSMENT
  7. DISCUSSION
  8. Acknowledgements
  9. REFERENCES
  10. Supporting Information
  • 1
    K. Knutson,J. Smith,M.A. Wallert,J.J. Provost ( 2009) 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 of malate dehydrogenase, green fluorescent protein.
  • 2
    B.B. Montelone,D.A. Rintoul,L.G. Williams ( 2008), Assessment of the effectiveness of the studio format in introductory undergraduate biology. Cell Biol. Educ. 7, 234242.
  • 3
    R. Boyer, ( 2003) Concepts and Skills in the Biochemistry/Molecular Biology Lab. BAMBED 31, 102105.
  • 4
    S.D. Domin, ( 1999) A review of laboratory instruction styles. J Chem. Educ. 76, 543547.
  • 5
    G.C. Weaver,C.B. Russel,D.J. Wink ( 2008) Inquiry-based and research-based laboratory pedagogies in undergraduate science. Nat. Chem. Biol. 4, 577480
  • 6
    H.A. Traver,M.J. Kalsher,J.J. Diwan,J.T. Warden ( 2001). Student reactions and learning: Evaluation of a biochemistry course that uses Web technology and student collaboration. BAMBED 29, 5053.
  • 7
    S.R. Goyette,J. DeLuca ( 2007) A semester-long student-directed research project involving enzyme immunoassay: Appropriate for immunology, endocrinology, or neuroscience courses. Cell Biol. Educ. 6, 332342.
  • 8
    D.B. Rivers, ( 2002) Using a course-long theme for inquiry-based laboratories in a comparative physiology course Adv. Phys. Ed. 26, 317326.
  • 9
    M.E. Rasche ( 2004) Outcomes of a research-driven laboratory and literature course designed to enhance undergraduate contributions to original research. BAMBED, 32, 101107.
  • 10
    J.E. Bell ( 2001). The future of education in the molecular life sciences. Nat. Rev. Mol. Cell. Biol. 2, 221225.
  • 11
    E. Martz ( 2002) Protein explorer: Easy yet powerful macromolecular visualization. Trends Biochem. Sci. 27, 107109; available athttp://proteinexplorer.org.
  • 12
    L. Grell,C. Parkin,L. Slatest,P.A. Craig ( 2006) EZ-Viz, a tool for simplifying molecular viewing in PyMOL. BAMBED 34, 402407.
  • 13
    A.E. Bednarski,S.C.R. Elgin,H.B. Pakrasi ( 2005) An Inquiry into protein structure and genetic disease: Introducing undergraduates to bioinformatics in a large introductory course. Cell Biol. Educ. 4, 207220.
  • 14
    T.L. Schneider,B.R. Linton ( 2008) Introduction to protein structure through genetic diseases. J. Chem. Educ. 85, 662665.
  • 15
    B. Cox,M.M. Chit,T. Weaver,C. Gietl,J. Bailey,E. Bell,L. Banaszak ( 2005) Organelle and translocatable forms of glyoxysomal malate dehydrogenase. The effect of the N-terminal presequence. FEBS J. 272, 643654.
  • 16
    C.R. Goward,D.J. Nicholls ( 1994) Malate dehydrogenase: A model for structure, evolution, and catalysis. Prot. Sci. 3, 18831888.
  • 17
    J.E. Bell,H.P. Yennawar,S.K. Wright,J.R. Thompson,R.E. Viola,L.J. Banaszak ( 2001) Structural analysis of a malate dehydrogenase with a variable active site. J. Biol. Chem. 276, 3115631162.
  • 18
    D. Ebert-May ( 2008) Classroom assessment techniques scoring rubrics, Dept of Plant Biology Michigan State University. Available at: http://www.flaguide.org/cat/rubrics/rubrics7.php; Retrieved 12 July,2008.
  • 19
    D. Lapatto ( 2007) Undergraduate research experiences support science career decisions and active learning. CBE Life Sci. Educ. 6. 297306
  • 20
    American Society for Biochemistry and Molecular Biology ( 2009) The Biochemistry and Molecular Biology Major and Liberal Education. Liberal Education Spring Ed., Washington, DC, pp. 613.

Supporting Information

  1. Top of page
  2. Abstract
  3. INTRODUCTION
  4. LABORATORY DESIGN
  5. GRADING
  6. ASSESSMENT
  7. DISCUSSION
  8. Acknowledgements
  9. REFERENCES
  10. Supporting Information

Additional Supporting Information may be found in the online version of this article.

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