BIOC2101 Principles of Biochemistry Scientific Report Assignment (worth 12%)

Scientific Report Assignment Learning Outcomes:

1. Write an abbreviated report in the style of a scientific journal article.

2. Use appropriate styles of writing and content to clearly distinguish between different sections of a
scientific report (aims, introduction, methods, results, discussion, references).
3. Use consistent structure and formatting that is appropriate for both text and data presentation
within a scientific report.
4. Manipulate a simple data set for formal presentation within a scientific report.
5. Analyse, interpret and discuss scientific data as it relates to the aims and context of a scientific
report.
6. Define and describe the significance of KM and Vmax values for an enzyme.
7. Determine KM and Vmax values of an enzyme using appropriate raw data and processing techniques.

BIOC2101 REPORT INSTRUCTIONS

Report Title: Determining the KM and Vmax of a Mystery Enzyme

PREMISE: You are a scientist who has isolated an enzyme from a biological sample. As part of your suite of
investigations to determine the role and identity of this enzyme, you decide to carry out a simple
experiment that will allow you to calculate the K M and Vmax of the enzyme. The data from your experiment
will be posted in a separate document in Moodle (in the ‘Scientific Report Assignment’ section). The data
sheet for your enzyme also contains some other basic information about your enzyme, but not its identity.

You are now required to write up a short scientific report that explains your experiment and the outcomes
of your investigation to your BIOC2101 class colleagues who will be peer reviewing your work. Please note
that there are several different enzymes being investigated, whereby each student is automatically
assigned a set of data for a specific mystery enzyme (the selection has already been performed for you; it
will be the only enzyme data sheet that you have access to in Moodle). But you should take this into
account when peer-reviewing your colleague’s reports, as not everyone will be working with the same data.

IMPORTANT: This is intended to be a simple report. The assignment has been designed to emphasise
best practice in scientific communication techniques and conventions for the development of associated
skills.
Instructions on how to write your report are provided below. Your report should consist of the following 6
sections: 1) Aims, 2) Introduction, 3) Methods, 4) Results, 5) Discussion, 6) References. Instructions on how
to write each section are provided below.

STRICT REPORT REQUIREMENTS

 DO NOT write your name or student number anywhere on your Draft Report. Your electronic
submission in Moodle will automatically provide your name to course instructors but the peer
review component of this assignment is anonymous and so requires that your identification is not
made visible in the report itself.
 Your submitted file must be in PDF format. Some file formats are not supported by other
computers when submitted for the peer review process. Therefore, it is essential that you submit a
file type that is recognised by all computers, in this case, PDF. If a peer reviewer cannot access your
 file due to an incorrect file type, you will miss out on valuable feedback and may also miss out on
marks.

GENERAL REPORT TIPS

 Use third person ‘style’ and past tense when writing your report.
 Use Arial or Calibri font no smaller than size 11 with 1.0 or 1.15 line spacing.
 Try to comply with recommended section lengths. If you exceed the recommended section length
significantly, you may lose marks if the extra work is not high quality and immediately relevant. If
you write a lot less that the recommended section length, you may lose marks if you have not fully
satisfied the essential requirements of the section.
 To standardise and simplify things, avoid using images and diagrams in your report. The only figures
should be tables and/or graphs in your Results section.

BIOC2101 Scientific Report Section Structure and Content Guide

1. Aims

 Section weighting: 2 marks

 Length: 1 or 2 sentences.
 Content: After your report title, briefly state the purpose of your experiment (i.e. to determine
specific properties (KM and Vmax) of the enzyme you have isolated; but use better wording than this
example). When describing the aim(s) of an experiment, it is also common to mention the basic
technique or approach that you have employed to conduct your investigation. For example: ‘The
aim of this investigation was to determine the concentration of haemoglobin in an unknown
solution using a spectrophotometric assay’. More information on the methods used in this
experiment can be found below in the ‘Methods’ section. HINT: Look at the abstracts of scientific
journal articles to help you achieve the appropriate professional tone and wording for your aim.
(But please note that your ‘Aims’ section does not have to be written in the style and structure of
an ‘Abstract’ which is typically longer than simply stating the aims of an experiment).

2. Introduction

 Section weighting: 3 marks

 Length: approximately half a page of text (about 1 – 3 paragraphs).
 Content: The introduction section of scientific reports gives background and context to an
investigation. Since this is a very simple report, there is no need to write a complex introduction. It
should simply contain basic definitions of the K M and Vmax of an enzyme, and a description of the
significance of KM values (i.e. why are they helpful to our understanding of how a particular enzyme
works?). It should then link this information to your aim of determining the K M and Vmax of your
isolated ‘mystery’ enzyme. Again, have a look at the introduction sections of scientific journal
articles to help you achieve the appropriate tone and style of your introduction.

3. Methods

 Section weighting: 3 marks

 Length: approximately half to 1 page of text.
 Content: Instead of including all the specific experimental details that would usually be included in
a scientific report or journal article (i.e. concentrations, volumes, step-by-step protocols, etc.),
provide a brief step-by-step description of the overall procedure used. A numbered list of steps is
the recommended format of this description so the reader can easily follow the procedure in the
correct sequence. Your write-up should allow a reader to understand the basic approach you used
in your investigation to achieve the desired outcomes. If your explanation is unclear, your peer
reviewer(s) should be able to explain why. HINT: Your enzyme data sheet will contain a very brief
explanation of the methods used. If you use this alone as your method by writing it in your own
words (as much as possible, anyway), you may only receive 1 or zero marks for this section. If you
go beyond this very simple explanation by including a few more details based on your learnings
from the Enzymes practical where you wrote up your own protocol, you may receive 2 or 3 marks
out of 3 for this section. Below are some extra tips to help you with the Methods section:
- This section is only titled ‘Methods’, so there is no need to list and describe the details of all
materials, reagents or reaction constituents etc.
- You do not know what your enzyme is and so you cannot comment on or guess the identity
of the substrate for your enzyme in your methods section (although you could possibly do
this in the discussion section). Yes, the substrate must have been known in order to carry
out the experiments that produced the data for your enzyme. But the purpose of this
assignment is to look at the results from another angle (i.e. working backwards), because
giving you the identity of the substrate would potentially give away the identity of your
enzyme and make the activity less compelling.
- You do not need to comment on concentrations, amounts, volumes, buffer identities or any
other details like these, as already outlined above.
- Think about the data you have been given that you will be using to calculate K M and Vmax
values in your report. You have substrate concentrations and initial reaction velocities.
There is no need to comment on how the range of substrate concentrations was selected,
but you SHOULD comment on how the initial reaction velocities were determined. HINT:
Look at the method and results for Part 2 of your Week 3 practical on Enzymes – you
determined an initial reaction velocity here. Try to describe that approach in a few
sentences only. That should help you ‘flesh-out’ or expand the ‘experimental method’ that
was already given in your enzyme data sheet. Other information and writing styles in the
Week 3 Enzymes practical notes may assist you with other aspect of the Methods section.
- Here is an example ‘Methods’ section that I wrote up for investigating the optimal pH of an
acid phosphatase enzyme. It gives you an indication of the style, depth and length of a
methods section that could score you full marks for this criterion:

Sample Method ‘Style’ (Written for a DIFFERENT Experiment):

Method for investigating the effect of pH on the activity of acid phosphatase

1. Seven reaction tubes were set up to contain a range of buffers varying in pH from 3 - 9.
2. Enzyme substrate was also added to each of the seven tubes (at the same
concentration in each tube).
3. A consistent volume of enzyme was then added to each tube at staggered 1-minute
intervals to start the reactions.
4. Each reaction was then stopped after the same duration of time by the addition of an
agent to denature the enzyme.
5. An additional tube was set up as the reaction ‘Blank’.
6. The blank was prepared by adding substrate and buffer at pH 5, followed by the
denaturing agent for the enzyme and then the enzyme itself, all mixed thoroughly.
7. Using a spectrophotometer, absorbance values were determined for all seven reaction
mixtures and the reaction blank. The blank value was then used to ‘correct’ the values
for the other seven reactions.
 8. These were compared with a standard curve for the reaction product to determine the
amount of product released during the reaction time.
9. A graph of enzyme activity (product released per reaction time) against pH was then
used to determine the optimal pH of the acid phosphatase (pH at which the enzyme
activity is highest).

4. Results

 Section weighting: 4 marks

 Length: approximately 1-2 pages, depending on how your data is presented.
 Content: In your results section:
- Include 1 data table containing both the raw data that you have been provided for the
report as well as processed versions of the data that you will need for determining K M and
Vmax of your enzyme. This data table can be prepared using Word or Excel, for example. You
can also include the other enzyme properties (provided in the data sheet) in this table, or
you can list them separately elsewhere in the Results section.
- Your results section should also contain 1 data graph that you have used for determining
Km and Vmax of your enzyme. This data graph can be prepared using graphing software like
Excel or Prism. Be sure to include all appropriate axes, titles and legends (if appropriate) for
your table and graph. (See helpful resources in Teams and Moodle to help you with the use
of Excel for this purpose).
- And lastly, your results section should contain a brief paragraph of text to accompany the
table and graph. The text should state what data is shown in the table and graph, explain
how it was processed to determine K M and Vmax, and state the final KM and Vmax values
determined for your enzyme. Remember that the purpose of a results section is to state
your results, indicating any significant outcomes or trends. Interpreting results and/or
discussing their significance in light of related literature is the purpose of the Discussion
section (below).

5. Discussion

 Section weighting: 4 marks

 Length: approximately half to 1 page.
 Content: In your discussion section:
- Briefly re-state the main outcomes of your investigation (i.e. the final K M and Vmax values
determined for your enzyme).
- Comment on whether you think the KM value of your enzyme might be high (mM range) or
low (µM range) in relation to the average K M values of enzymes. (There are clear statements
relating to these parameters in your recommended text for the course and other similar
text and online resources). At this point, you can also comment on the relative binding
affinity of your enzyme for its substrate based on the K M value that you determined,
especially if it is particularly high or low.
- For this report, you were also provided with other properties that were pre-determined for
your ‘mystery’ enzyme. Combine these properties with the K M value that you determined
to see if you can identify your ‘mystery’ enzyme based on these few pieces of information.
Please note that this is only a guess! There may be more than one answer, or you may not
find any enzyme that matches. Just use the information you have to search online literature
and other resources and see what you can find. (PLEASE NOTE: the properties of your
enzyme (on the data sheet) are based on those of a common enzyme, but the experimental
data provided has been arbitrarily generated to provide you with the correct K M value for
your enzyme if you process the data correctly. Enzyme isoforms, species of origin, and
 enzymatic conditions all affect the K M value of a given reaction, but clearly we are not taking
these things into account in this activity. The purpose of trying to ‘guess’ the identity of
your enzyme based on very limited information is only to help you better engage with the
learning outcomes of the assignment). TIP: Check biochemistry text-books and other general
sources of information on KM values, as all the enzymes studied in this investigation have been very
well characterised and so should be relatively easy to find if you determined the correct K M value ; )

6. References

 Section weighting: 2 marks

 Length: dependent on the number of references you have used.
 Content: In the writing of your report, you should use a minimum of 3 peer-reviewed scientific
literature articles (and at least 2 of these should be primary research articles). Primary research
articles are best when discussing your experimental outcomes, but review articles can be helpful
for providing more generalised perspectives. Other sources of information can also be cited, such
as textbooks and websites, but aim to use resources from well-known or reputable organisations.
Do not cite course lecture notes (unless the lecturer is the primary source of the original
information, which is rare). There should also be no need to reference the BIOC2101 course
practical notes.
 Style: Please use the referencing style employed in the journal ‘Nature’ because it is a good
example of an appropriate referencing style to use for this report. Here is an example of a sentence
with a ‘Nature’ style internal reference in it, followed immediately by how the reference would look
in your references list:

‘Despite popular belief that fat-burning pills will cause weight loss, Hoehn and colleagues definitively
showed that increasing fat oxidation alone is not sufficient to reverse or prevent obesity 1.’

References
1 Hoehn, K. L. et al. Acute or chronic upregulation of mitochondrial fatty acid oxidation has no net
effect on whole-body energy expenditure or adiposity. Cell metabolism 11, 70-76,
doi:10.1016/j.cmet.2009.11.008 (2010).

The End – Happy Reporting!